STAU2_MOUSE
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 03-AUG-2022, entry version 149.
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}.
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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; 12.
DR IntAct; Q8CJ67; 3.
DR MINT; Q8CJ67; -.
DR STRING; 10090.ENSMUSP00000124505; -.
DR iPTMnet; Q8CJ67; -.
DR PhosphoSitePlus; Q8CJ67; -.
DR MaxQB; Q8CJ67; -.
DR PaxDb; Q8CJ67; -.
DR PeptideAtlas; Q8CJ67; -.
DR PRIDE; 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 Antibodypedia; 1305; 241 antibodies from 25 providers.
DR DNASU; 29819; -.
DR Ensembl; ENSMUST00000027052; ENSMUSP00000027052; ENSMUSG00000025920. [Q8CJ67-2]
DR Ensembl; ENSMUST00000054668; ENSMUSP00000053190; ENSMUSG00000025920. [Q8CJ67-1]
DR Ensembl; ENSMUST00000115359; ENSMUSP00000111016; ENSMUSG00000025920. [Q8CJ67-5]
DR Ensembl; ENSMUST00000144138; ENSMUSP00000119130; ENSMUSG00000025920. [Q8CJ67-5]
DR Ensembl; ENSMUST00000159558; ENSMUSP00000125726; ENSMUSG00000025920. [Q8CJ67-3]
DR Ensembl; ENSMUST00000162007; ENSMUSP00000124303; ENSMUSG00000025920. [Q8CJ67-3]
DR Ensembl; ENSMUST00000162435; ENSMUSP00000123827; ENSMUSG00000025920. [Q8CJ67-2]
DR Ensembl; ENSMUST00000162627; ENSMUSP00000123781; ENSMUSG00000025920. [Q8CJ67-2]
DR Ensembl; ENSMUST00000162751; ENSMUSP00000124505; ENSMUSG00000025920. [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 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; EGMANNI; -.
DR OrthoDB; 823092at2759; -.
DR PhylomeDB; Q8CJ67; -.
DR TreeFam; TF350296; -.
DR BioGRID-ORCS; 29819; 1 hit in 72 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 262 other tissues.
DR ExpressionAtlas; Q8CJ67; baseline and differential.
DR Genevisible; Q8CJ67; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; 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; ISO:MGI.
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:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR CDD; cd19880; DSRM_STAU2_rpt1; 1.
DR CDD; cd19882; DSRM_STAU2_rpt2; 1.
DR CDD; cd19884; DSRM_STAU2_rpt3; 1.
DR CDD; cd19886; DSRM_STAU2_rpt4; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR044476; STAU2_DSRM_1.
DR InterPro; IPR044464; STAU2_DSRM_2.
DR InterPro; IPR044473; STAU2_DSRM_3.
DR InterPro; IPR044474; STAU2_DSRM_4.
DR InterPro; IPR032478; Staufen_C.
DR Pfam; PF00035; dsrm; 4.
DR Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 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
