ID STAU2_MOUSE Reviewed; 570 AA. AC Q8CJ67; Q8BSY8; Q8CJ66; Q8R175; Q91Z19; Q9D5N7; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JUL-2024, entry version 160. DE RecName: Full=Double-stranded RNA-binding protein Staufen homolog 2; GN Name=Stau2; 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] (ISOFORMS 1 AND 2), RNA-BINDING, DOMAIN, AND RP TISSUE SPECIFICITY. RC STRAIN=BALB/cJ; RX PubMed=12140260; DOI=10.1242/jcs.115.16.3285; RA Duchaine T.F., Hemraj I., Furic L., Deitinghoff A., Kiebler M.A., RA DesGroseillers L.; RT "Staufen2 isoforms localize to the somatodendritic domain of neurons and RT interact with different organelles."; RL J. Cell Sci. 115:3285-3295(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5). RC STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, Placenta, and Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 42-570 (ISOFORMS 1/2). RC STRAIN=FVB/N; 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 [4] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=12859680; DOI=10.1046/j.1471-4159.2003.01883.x; RA Belanger G., Stocksley M.A., Vandromme M., Schaeffer L., Furic L., RA DesGroseillers L., Jasmin B.J.; RT "Localization of the RNA-binding proteins Staufen1 and Staufen2 at the RT mammalian neuromuscular junction."; RL J. Neurochem. 86:669-677(2003). RN [5] RP INTERACTION WITH XPO5, SUBCELLULAR LOCATION, DOMAIN NLS 1, AND MUTAGENESIS RP OF HIS-235; LYS-237; 273-LYS-LYS-274 AND 289-LYS--ARG-291. RX PubMed=15166236; DOI=10.1074/jbc.c400226200; RA Macchi P., Brownawell A.M., Grunewald B., DesGroseillers L., Macara I.G., RA Kiebler M.A.; RT "The brain-specific double-stranded RNA-binding protein Staufen2: nucleolar RT accumulation and isoform-specific exportin-5-dependent export."; RL J. Biol. Chem. 279:31440-31444(2004). RN [6] RP STRUCTURE BY NMR OF 308-383. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of DSRNA binding domain in Staufen homolog 2."; RL Submitted (JUL-2003) to the PDB data bank. CC -!- FUNCTION: RNA-binding protein required for the microtubule-dependent CC transport of neuronal RNA from the cell body to the dendrite. As CC protein synthesis occurs within the dendrite, the localization of CC specific mRNAs to dendrites may be a prerequisite for neurite outgrowth CC and plasticity at sites distant from the cell body (By similarity). CC {ECO:0000250|UniProtKB:Q68SB1}. CC -!- SUBUNIT: Interacts with microtubules. Isoform 2 and isoform 3 may also CC interact with ribosomes, and this association is independent of CC translation (By similarity). Identified in a mRNP complex, at least CC composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, CC PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with the exportin CC XPO5. This requires RNA and RAN bound to GTP. Interacts with TRIM71 CC (via NHL repeats) in an RNA-dependent manner (By similarity). CC {ECO:0000250|UniProtKB:Q68SB1, ECO:0000250|UniProtKB:Q9NUL3, CC ECO:0000269|PubMed:15166236}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15166236}. Nucleus CC {ECO:0000269|PubMed:15166236}. Nucleus, nucleolus CC {ECO:0000269|PubMed:15166236}. Endoplasmic reticulum CC {ECO:0000269|PubMed:15166236}. Note=Shuttles between the nucleolus, CC nucleus and the cytoplasm. Nuclear export of isoform 1 is independent CC of XPO1/CRM1 and requires the exportin XPO5. Nuclear export of isoform CC 2 and isoform 3 can occur by both XPO1/CRM1-dependent and XPO1/CRM1- CC independent pathways. May also be found in large cytoplasmic CC ribonucleoprotein (RNP) granules which are present in the actin rich CC regions of myelinating processes and associated with microtubules, CC polysomes and the endoplasmic reticulum. Also recruited to stress CC granules (SGs) upon inhibition of translation or oxidative stress. CC These structures are thought to harbor housekeeping mRNAs when CC translation is aborted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=Long; CC IsoId=Q8CJ67-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=Q8CJ67-2; Sequence=VSP_015379, VSP_015380; CC Name=3; CC IsoId=Q8CJ67-3; Sequence=VSP_015379, VSP_015380, VSP_015383, CC VSP_015384; CC Name=4; CC IsoId=Q8CJ67-4; Sequence=VSP_015378, VSP_015383, VSP_015384; CC Name=5; CC IsoId=Q8CJ67-5; Sequence=VSP_015381, VSP_015382; CC -!- TISSUE SPECIFICITY: Expressed in brain and neurons, where isoform 2 and CC isoform 3 appear to be the most abundant. Expressed at the CC neuromuscular junction of the extensor digitorum longus, tibialis CC anterior and soleus muscles. Expression at neuromuscular junctions is CC most pronounced in slow-twitch muscle. Also weakly expressed in heart, CC kidney, ovary and testis. {ECO:0000269|PubMed:12140260, CC ECO:0000269|PubMed:12859680}. CC -!- INDUCTION: Expression in extrasynaptic regions of muscle is induced by CC denervation. Expression in myoblasts is induced during differentiation CC into myotubes and by treatment with nerve derived trophic factors such CC as AGRN (agrin) and NRG1 (neuregulin). {ECO:0000269|PubMed:12859680}. CC -!- DOMAIN: The DRBM 3 domain appears to be the major RNA-binding CC determinant. This domain also mediates interaction with XPO5 and is CC required for XPO1/CRM1-independent nuclear export. CC {ECO:0000269|PubMed:12140260, ECO:0000269|PubMed:15166236}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF459099; AAN37928.1; -; mRNA. DR EMBL; AF459100; AAN37929.1; -; mRNA. DR EMBL; AK015087; BAB29708.1; -; mRNA. DR EMBL; AK028390; BAC25926.1; -; mRNA. DR EMBL; BC010300; AAH10300.1; -; mRNA. DR EMBL; BC025118; AAH25118.1; -; mRNA. DR CCDS; CCDS14831.2; -. [Q8CJ67-1] DR CCDS; CCDS48223.1; -. [Q8CJ67-2] DR CCDS; CCDS83529.1; -. [Q8CJ67-3] DR RefSeq; NP_001104742.1; NM_001111272.1. [Q8CJ67-2] DR RefSeq; NP_001333974.1; NM_001347045.1. [Q8CJ67-3] DR RefSeq; NP_079579.2; NM_025303.3. [Q8CJ67-1] DR RefSeq; XP_006495591.1; XM_006495528.3. [Q8CJ67-1] DR RefSeq; XP_006495595.1; XM_006495532.3. [Q8CJ67-2] DR RefSeq; XP_011236689.1; XM_011238387.1. [Q8CJ67-1] DR RefSeq; XP_011236691.1; XM_011238389.1. [Q8CJ67-2] DR RefSeq; XP_017176591.1; XM_017321102.1. [Q8CJ67-1] DR PDB; 1UHZ; NMR; -; A=308-383. DR PDBsum; 1UHZ; -. DR AlphaFoldDB; Q8CJ67; -. DR SMR; Q8CJ67; -. DR BioGRID; 205899; 19. DR IntAct; Q8CJ67; 3. DR MINT; Q8CJ67; -. DR STRING; 10090.ENSMUSP00000124505; -. DR GlyGen; Q8CJ67; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q8CJ67; -. DR PhosphoSitePlus; Q8CJ67; -. DR PaxDb; 10090-ENSMUSP00000124505; -. DR PeptideAtlas; Q8CJ67; -. DR ProteomicsDB; 254582; -. [Q8CJ67-1] DR ProteomicsDB; 254583; -. [Q8CJ67-2] DR ProteomicsDB; 254584; -. [Q8CJ67-3] DR ProteomicsDB; 254585; -. [Q8CJ67-4] DR ProteomicsDB; 254586; -. [Q8CJ67-5] DR Pumba; Q8CJ67; -. DR Antibodypedia; 1305; 262 antibodies from 25 providers. DR DNASU; 29819; -. DR Ensembl; ENSMUST00000027052.13; ENSMUSP00000027052.7; ENSMUSG00000025920.20. [Q8CJ67-2] DR Ensembl; ENSMUST00000054668.13; ENSMUSP00000053190.7; ENSMUSG00000025920.20. [Q8CJ67-1] DR Ensembl; ENSMUST00000115359.10; ENSMUSP00000111016.4; ENSMUSG00000025920.20. [Q8CJ67-5] DR Ensembl; ENSMUST00000144138.4; ENSMUSP00000119130.3; ENSMUSG00000025920.20. [Q8CJ67-5] DR Ensembl; ENSMUST00000159558.8; ENSMUSP00000125726.2; ENSMUSG00000025920.20. [Q8CJ67-3] DR Ensembl; ENSMUST00000162007.8; ENSMUSP00000124303.2; ENSMUSG00000025920.20. [Q8CJ67-3] DR Ensembl; ENSMUST00000162435.8; ENSMUSP00000123827.2; ENSMUSG00000025920.20. [Q8CJ67-2] DR Ensembl; ENSMUST00000162627.8; ENSMUSP00000123781.2; ENSMUSG00000025920.20. [Q8CJ67-2] DR Ensembl; ENSMUST00000162751.8; ENSMUSP00000124505.2; ENSMUSG00000025920.20. [Q8CJ67-1] DR GeneID; 29819; -. DR KEGG; mmu:29819; -. DR UCSC; uc007ajn.2; mouse. [Q8CJ67-1] DR UCSC; uc007ajo.2; mouse. [Q8CJ67-2] DR UCSC; uc007ajq.2; mouse. [Q8CJ67-3] DR UCSC; uc007ajr.2; mouse. [Q8CJ67-5] DR AGR; MGI:1352508; -. DR CTD; 27067; -. DR MGI; MGI:1352508; Stau2. DR VEuPathDB; HostDB:ENSMUSG00000025920; -. DR eggNOG; KOG3732; Eukaryota. DR GeneTree; ENSGT00940000154977; -. DR HOGENOM; CLU_162785_0_0_1; -. DR InParanoid; Q8CJ67; -. DR OMA; KTIVKXV; -. DR OrthoDB; 2882160at2759; -. DR PhylomeDB; Q8CJ67; -. DR TreeFam; TF350296; -. DR BioGRID-ORCS; 29819; 1 hit in 77 CRISPR screens. DR ChiTaRS; Stau2; mouse. DR EvolutionaryTrace; Q8CJ67; -. DR PRO; PR:Q8CJ67; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q8CJ67; Protein. DR Bgee; ENSMUSG00000025920; Expressed in embryonic brain and 265 other cell types or tissues. DR ExpressionAtlas; Q8CJ67; baseline and differential. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC. DR GO; GO:0043198; C:dendritic shaft; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI. DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI. DR GO; GO:0019894; F:kinesin binding; ISO:MGI. DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0043022; F:ribosome binding; ISO:MGI. DR GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; ISO:MGI. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0048592; P:eye morphogenesis; ISO:MGI. DR GO; GO:0007281; P:germ cell development; IBA:GO_Central. DR GO; GO:0008298; P:intracellular mRNA localization; IBA:GO_Central. DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI. DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISO:MGI. DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:MGI. DR GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI. DR GO; GO:0051489; P:regulation of filopodium assembly; ISO:MGI. DR CDD; cd19882; DSRM_STAU2_rpt2; 1. DR CDD; cd19884; DSRM_STAU2_rpt3; 1. DR CDD; cd19886; DSRM_STAU2_rpt4; 1. DR Gene3D; 3.30.160.20; -; 4. DR Gene3D; 6.10.250.1360; -; 1. DR InterPro; IPR051740; DRBM-containing_protein. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR044464; STAU2_DSRM_2. DR InterPro; IPR044473; STAU2_DSRM_3. DR InterPro; IPR044474; STAU2_DSRM_4. DR InterPro; IPR032478; Staufen_C. DR PANTHER; PTHR46054:SF1; DOUBLE-STRANDED RNA-BINDING PROTEIN STAUFEN HOMOLOG 2; 1. DR PANTHER; PTHR46054; MATERNAL EFFECT PROTEIN STAUFEN; 1. DR Pfam; PF00035; dsrm; 4. DR Pfam; PF16482; Staufen_C; 1. DR SMART; SM00358; DSRM; 4. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 4. DR PROSITE; PS50137; DS_RBD; 4. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Endoplasmic reticulum; KW Microtubule; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW RNA-binding; Transport. FT CHAIN 1..570 FT /note="Double-stranded RNA-binding protein Staufen homolog FT 2" FT /id="PRO_0000072247" FT DOMAIN 8..75 FT /note="DRBM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT DOMAIN 95..181 FT /note="DRBM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT DOMAIN 207..274 FT /note="DRBM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT DOMAIN 307..375 FT /note="DRBM 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT REGION 71..94 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 178..203 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 381..570 FT /note="Required for dendritic transport" FT /evidence="ECO:0000250" FT REGION 381..413 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 545..570 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 273..291 FT /note="Nuclear localization signal 1" FT MOTIF 373..412 FT /note="Nuclear localization signal 2" FT /evidence="ECO:0000250" FT COMPBIAS 553..570 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9NUL3" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9NUL3" FT MOD_RES 405 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9NUL3" FT MOD_RES 416 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9NUL3" FT MOD_RES 426 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9NUL3" FT MOD_RES 440 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9NUL3" FT MOD_RES 455 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9NUL3" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9NUL3" FT VAR_SEQ 1..305 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_015378" FT VAR_SEQ 1..32 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12140260, FT ECO:0000303|PubMed:15489334" FT /id="VSP_015379" FT VAR_SEQ 33..38 FT /note="GPAHSK -> MLQINQ (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12140260, FT ECO:0000303|PubMed:15489334" FT /id="VSP_015380" FT VAR_SEQ 92..125 FT /note="GSITPTVELNGLAMKRGEPAIYRPLDPKPFPNYR -> VGKLKETVLSPAHE FT VMIVGITHYSADNFFLHWCL (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_015381" FT VAR_SEQ 126..570 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_015382" FT VAR_SEQ 511 FT /note="A -> V (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_015383" FT VAR_SEQ 512..570 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_015384" FT MUTAGEN 235 FT /note="H->A: Abrogates RNA-binding by DRBM 3 and FT interaction with XPO5 and nuclear export; when associated FT with A-237." FT /evidence="ECO:0000269|PubMed:15166236" FT MUTAGEN 237 FT /note="K->A: Abrogates RNA-binding by DRBM 3 and FT interaction with XPO5 and nuclear export; when associated FT with A-235." FT /evidence="ECO:0000269|PubMed:15166236" FT MUTAGEN 273..274 FT /note="KK->AA: Prevents nuclear localization of mutants FT lacking DRBM 3 function; when associated with 289-AAA-291." FT /evidence="ECO:0000269|PubMed:15166236" FT MUTAGEN 289..291 FT /note="KKR->AAA: Prevents nuclear localization of mutants FT lacking DRBM 3 function; when associated with 257-AA-258." FT /evidence="ECO:0000269|PubMed:15166236" FT HELIX 308..318 FT /evidence="ECO:0007829|PDB:1UHZ" FT STRAND 325..333 FT /evidence="ECO:0007829|PDB:1UHZ" FT STRAND 339..346 FT /evidence="ECO:0007829|PDB:1UHZ" FT STRAND 349..357 FT /evidence="ECO:0007829|PDB:1UHZ" FT HELIX 358..373 FT /evidence="ECO:0007829|PDB:1UHZ" FT HELIX 377..383 FT /evidence="ECO:0007829|PDB:1UHZ" SQ SEQUENCE 570 AA; 62535 MW; 3D7F2DA66B0B8D57 CRC64; MANPKEKTPV CLVNELARFH SIQPQYKLLN ESGPAHSKMF SVQLSLGEQT WESEGSSIKK AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PGSITPTVEL NGLAMKRGEP AIYRPLDPKP FPNYRANYNF RGMYNQRYHC PMPKIFYVQL TVGNNEFFGE GKTRQAARHN AAMKALQALQ NEPIPEKSPQ NGESGKEMDD DKDANKSEIS LVFEIALKRN MPVSFEVIKE SGPPHMKSFV TRVSVGEFSA EGEGNSKKLS KKRAATTVLQ ELKKLPPLPV VEKPKLFFKK RPKTIVKAGP DYGQGMNPIS RLAQIQQARK EKEPDYILLS ERGMPRRREF VMQVKVGNEV ATGTGPNKKI AKKNAAEAML LQLGYKASTS LQDPLDKTGE NKGWSGPKPG FPEPTNNTPK GILHLSPDVY QEMEASRHRV TSGTTLSYLS PKDMNQPSSS FFSVSPSSTS SATVARELLM NGTSPTAEAI GLKGSSPTSP CSSVQPSKQL EYLARIQGFQ AALSALKQFS EQGLESIDGA VNVEKGSLEK QAKHLREKAD NNQAKPASIS QDCKKSKSAI //