(data stored in ACNUC7421 zone)

SWISSPROT: DDX3X_MOUSE

ID   DDX3X_MOUSE             Reviewed;         662 AA.
AC   Q62167; O09060; O09143;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 185.
DE   RecName: Full=ATP-dependent RNA helicase DDX3X;
DE            EC=3.6.4.13;
DE   AltName: Full=D1Pas1-related sequence 2;
DE   AltName: Full=DEAD box RNA helicase DEAD3;
DE            Short=mDEAD3;
DE   AltName: Full=DEAD box protein 3, X-chromosomal;
DE   AltName: Full=Embryonic RNA helicase;
GN   Name=Ddx3x; Synonyms=D1Pas1-rs2, Ddx3, Dead3, Erh;
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].
RC   STRAIN=C57BL/6J, and DBA;
RX   PubMed=8948440; DOI=10.1042/bj3080839;
RA   Sowden J.C., Putt W., Morrison K., Beddington R., Edwards Y.;
RT   "The embryonic RNA helicase gene (ERH): a new member of the DEAD box family
RT   of RNA helicases.";
RL   Biochem. J. 308:839-846(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Erythroleukemia;
RX   PubMed=8144024; DOI=10.1016/0378-1119(94)90541-x;
RA   Gee S.L., Conboy J.G.;
RT   "Mouse erythroid cells express multiple putative RNA helicase genes
RT   exhibiting high sequence conservation from yeast to mammals.";
RL   Gene 140:171-177(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT SER-2.
RX   PubMed=10859333; DOI=10.1084/jem.191.12.2083;
RA   Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J.,
RA   Lopez de Castro J.A.;
RT   "An N-acetylated natural ligand of human histocompatibility leukocyte
RT   antigen (HLA)-B39. Classical major histocompatibility complex class I
RT   proteins bind peptides with a blocked NH(2) terminus in vivo.";
RL   J. Exp. Med. 191:2083-2092(2000).
RN   [4]
RP   PROTEIN SEQUENCE OF 535-548, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and 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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [9]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-101; ARG-110 AND ARG-632, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
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   [10]
RP   INTERACTION WITH DHX33.
RX   PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA   Zhang Y., You J., Wang X., Weber J.;
RT   "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL   Mol. Cell. Biol. 35:2918-2931(2015).
CC   -!- FUNCTION: Multifunctional ATP-dependent RNA helicase. The ATPase
CC       activity can be stimulated by various ribo- and deoxynucleic acids
CC       indicative for a relaxed substrate specificity. In vitro can unwind
CC       partially double-stranded DNA with a preference for 5'-single-stranded
CC       DNA overhangs. Is involved in several steps of gene expression, such as
CC       transcription, mRNA maturation, mRNA export and translation. However,
CC       the exact mechanisms are not known and some functions may be specific
CC       for a subset of mRNAs. Involved in transcriptional regulation. Can
CC       enhance transcription from the CDKN1A/WAF1 promoter in a SP1-dependent
CC       manner. Found associated with the E-cadherin promoter and can down-
CC       regulate transcription from the promoter. Involved in regulation of
CC       translation initiation. Proposed to be involved in positive regulation
CC       of translation such as of cyclin E1/CCNE1 mRNA and specifically of
CC       mRNAs containing complex secondary structures in their 5'UTRs; these
CC       functions seem to require RNA helicase activity. Specifically promotes
CC       translation of a subset of viral and cellular mRNAs carrying a
CC       5'proximal stem-loop structure in their 5'UTRs and cooperates with the
CC       eIF4F complex. Proposed to act prior to 43S ribosomal scanning and to
CC       locally destabilize these RNA structures to allow recognition of the
CC       mRNA cap or loading onto the 40S subunit. After association with 40S
CC       ribosomal subunits seems to be involved in the functional assembly of
CC       80S ribosomes; the function seems to cover translation of mRNAs with
CC       structured and non-structured 5'UTRs and is independent of RNA helicase
CC       activity. Also proposed to inhibit cap-dependent translation by
CC       competetive interaction with EIF4E which can block the EIF4E:EIF4G
CC       complex formation. Proposed to be involved in stress response and
CC       stress granule assembly; the function is independent of RNA helicase
CC       activity and seems to involve association with EIF4E. May be involved
CC       in nuclear export of specific mRNAs but not in bulk mRNA export via
CC       interactions with XPO1 and NXF1. Also associates with polyadenylated
CC       mRNAs independently of NXF1. Associates with spliced mRNAs in an exon
CC       junction complex (EJC)-dependent manner and seems not to be directly
CC       involved in splicing. May be involved in nuclear mRNA export by
CC       association with DDX5 and regulating its nuclear location. Involved in
CC       innate immune signaling promoting the production of type I interferon
CC       (IFN-alpha and IFN-beta); proposed to act as viral RNA sensor,
CC       signaling intermediate and transcriptional coactivator. Involved in
CC       TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction,
CC       plays a role of scaffolding adapter that links IKBKE and IRF3 and
CC       coordinates their activation. Also found associated with IFNB
CC       promoters; the function is independent of IRF3. Can bind to viral RNAs
CC       and via association with MAVS/IPS1 and DDX58/RIG-I is thought to induce
CC       signaling in early stages of infection. Involved in regulation of
CC       apoptosis. May be required for activation of the intrinsic but inhibit
CC       activation of the extrinsic apoptotic pathway. Acts as an antiapoptotic
CC       protein through association with GSK3A/B and BIRC2 in an apoptosis
CC       antagonizing signaling complex; activation of death receptors promotes
CC       caspase-dependent cleavage of BIRC2 and DDX3X and relieves the
CC       inhibition. May be involved in mitotic chromosome segregation. Is an
CC       allosteric activator of CSNK1E, it stimulates CSNK1E-mediated
CC       phosphorylation of DVL2 and is involved in the positive regulation of
CC       canonical Wnt signaling (By similarity).
CC       {ECO:0000250|UniProtKB:O00571}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Binds RNA as a monomer at low DDX3X concentrations and as a
CC       dimer at high DDX3X concentrations. Interacts with XPO1, TDRD3, PABPC1,
CC       NXF1, EIF3C, MAVS, DDX58 and NCAPH. Interacts with DDX5; the
CC       interaction is regulated by the phosphorylation status of both
CC       proteins. Interacts with EIF4E; DDX3X competes with EIF4G1/EIF4G3 for
CC       interaction with EIF4E. Interacts with IKBKE; the interaction is
CC       direct. Interacts with IRF3; the interaction allows the phosphorylation
CC       and activation of IRF3 by IKBKE. Interacts with TBK1. Associates with
CC       the eukaryotic translation initiation factor 3 (eIF-3) complex.
CC       Associates with the 40S ribosome. Identified in a mRNP complex, at
CC       least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1,
CC       PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with SP1.
CC       Interacts with GSK3A, GSK3B and TNFRSF10B. Interacts with CSNK1E; the
CC       interaction enhances CSNK1E recruitment to DVL2. Interacts with DHX33;
CC       the interaction is independent of RNA (PubMed:26100019). Interacts with
CC       ERCC6 (By similarity). {ECO:0000250|UniProtKB:O00571,
CC       ECO:0000269|PubMed:26100019}.
CC   -!- INTERACTION:
CC       Q9UHD2:TBK1 (xeno); NbExp=8; IntAct=EBI-773173, EBI-356402;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}. Note=Located
CC       predominantly in nuclear speckles and, at low levels, throughout the
CC       cytoplasm. Located to the outer side of nuclear pore complexes (NPC).
CC       Shuttles between the nucleus and the cytoplasm in a XPO1 and may be
CC       also in a NFX1-dependent manner. Associated with polyadenylated mRNAs
CC       in the cytoplasm and the nucleus. Predominantly located in nucleus
CC       during G(0) phase and in the cytoplasm during G1/S phase (By
CC       similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Developmentally regulated.
CC   -!- DEVELOPMENTAL STAGE: Expressed in oocytes. Ubiquitously found in 9 days
CC       post-conception embryo, at later stages it is restricted to brain and
CC       kidney.
CC   -!- PTM: Phosphorylated by TBK1; the phosphorylation is required to
CC       synergize with TBK1 in IFN-beta induction. Probably also phosphorylated
CC       by IKBKE (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC       subfamily. {ECO:0000305}.
DR   EMBL; Z38117; CAA86261.1; -; mRNA.
DR   EMBL; L25126; AAA53630.1; -; mRNA.
DR   CCDS; CCDS30027.1; -.
DR   PIR; I84741; I84741.
DR   RefSeq; NP_034158.1; NM_010028.3.
DR   SMR; Q62167; -.
DR   BioGrid; 199084; 11.
DR   IntAct; Q62167; 16.
DR   MINT; Q62167; -.
DR   STRING; 10090.ENSMUSP00000000804; -.
DR   ChEMBL; CHEMBL3751657; -.
DR   iPTMnet; Q62167; -.
DR   PhosphoSitePlus; Q62167; -.
DR   SwissPalm; Q62167; -.
DR   REPRODUCTION-2DPAGE; Q62167; -.
DR   EPD; Q62167; -.
DR   jPOST; Q62167; -.
DR   MaxQB; Q62167; -.
DR   PaxDb; Q62167; -.
DR   PRIDE; Q62167; -.
DR   Ensembl; ENSMUST00000000804; ENSMUSP00000000804; ENSMUSG00000000787.
DR   GeneID; 13205; -.
DR   KEGG; mmu:13205; -.
DR   UCSC; uc009srl.2; mouse.
DR   CTD; 1654; -.
DR   MGI; MGI:103064; Ddx3x.
DR   eggNOG; KOG0335; Eukaryota.
DR   eggNOG; ENOG410XNTI; LUCA.
DR   GeneTree; ENSGT00940000154443; -.
DR   HOGENOM; HOG000268804; -.
DR   InParanoid; Q62167; -.
DR   KO; K11594; -.
DR   OMA; CYRSWVR; -.
DR   OrthoDB; 595675at2759; -.
DR   PhylomeDB; Q62167; -.
DR   TreeFam; TF300332; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   ChiTaRS; Ddx3x; mouse.
DR   PRO; PR:Q62167; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q62167; protein.
DR   Bgee; ENSMUSG00000000787; Expressed in 323 organ(s), highest expression level in secondary oocyte.
DR   ExpressionAtlas; Q62167; baseline and differential.
DR   Genevisible; Q62167; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:Ensembl.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0072559; C:NLRP3 inflammasome complex; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0043273; F:CTPase activity; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0008190; F:eukaryotic initiation factor 4E binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; ISO:MGI.
DR   GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
DR   GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR   GO; GO:0033592; F:RNA strand annealing activity; ISO:MGI.
DR   GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0031369; F:translation initiation factor binding; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
DR   GO; GO:0071470; P:cellular response to osmotic stress; ISS:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR   GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042256; P:mature ribosome assembly; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0031333; P:negative regulation of protein complex assembly; ISS:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR   GO; GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR   GO; GO:0031053; P:primary miRNA processing; IDA:MGI.
DR   GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
DR   GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR   GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
DR   GO; GO:0034063; P:stress granule assembly; IMP:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; ISO:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; ISO:MGI.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q62167.
DR   SWISS-2DPAGE; Q62167.
KW   Acetylation; Apoptosis; ATP-binding; Chromosome partition; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Helicase; Hydrolase; Immunity;
KW   Innate immunity; Isopeptide bond; Membrane; Methylation; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; Transcription;
KW   Transcription regulation; Translation regulation; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10859333"
FT   CHAIN           2..662
FT                   /note="ATP-dependent RNA helicase DDX3X"
FT                   /id="PRO_0000055010"
FT   DOMAIN          211..403
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          414..575
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         200..207
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   NP_BIND         224..231
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          2..139
FT                   /note="Required for TBK1 and IKBKE-dependent IFN-beta
FT                   activation"
FT                   /evidence="ECO:0000250"
FT   REGION          2..100
FT                   /note="Interaction with EIF4E"
FT                   /evidence="ECO:0000250"
FT   REGION          100..662
FT                   /note="Interaction with GSK3B"
FT                   /evidence="ECO:0000250"
FT   REGION          100..110
FT                   /note="Required for interaction with IKBKE"
FT                   /evidence="ECO:0000250"
FT   REGION          250..259
FT                   /note="Involved in stimulation of ATPase activity by DNA
FT                   and RNA, nucleic acid binding and unwinding"
FT                   /evidence="ECO:0000250"
FT   REGION          260..517
FT                   /note="Necessary for interaction with XPO1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           180..208
FT                   /note="Q motif"
FT   MOTIF           347..350
FT                   /note="DEAD box"
FT   COMPBIAS        582..662
FT                   /note="Gly/Ser-rich"
FT   COMPBIAS        609..616
FT                   /note="Poly-Ser"
FT   COMPBIAS        624..630
FT                   /note="Poly-Gly"
FT   COMPBIAS        633..641
FT                   /note="Poly-Gly"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:10859333"
FT   MOD_RES         55
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:23806337"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         101
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         104
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:15592455"
FT   MOD_RES         110
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         118
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17242355"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62095"
FT   MOD_RES         592
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         605
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         612
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         617
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
FT   MOD_RES         632
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   CROSSLNK        215
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00571"
SQ   SEQUENCE   662 AA;  73101 MW;  216515CB00324017 CRC64;
     MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK GFYDKDSSGW
     SSSKDKDAYS SFGSRGDSRG KSSFFGDRGS GSRGRFDDRG RGDYDGIGGR GDRSGFGKFE
     RGGNSRWCDK SDEDDWSKPL PPSERLEQEL FSGGNTGINF EKYDDIPVEA TGNNCPPHIE
     SFSDVEMGEI IMGNIELTRY TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS
     QIYADGPGEA LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV
     YGGAEIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD RMLDMGFEPQ
     IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY IFLAVGRVGS TSENITQKVV
     WVEEIDKRSF LLDLLNATGK DSLTLVFVET KKGADSLEDF LYHEGYACTS IHGDRSQRDR
     EEALHQFRSG KSPILVATAV AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL
     ATSFFNERNI NITKDLLDLL VEAKQEVPSW LENMAFEHHY KGSSRGRSKS SRFSGGFGAR
     DYRQSSGASS SSFSSSRASS SRSGGGGHGG SRGFGGGGYG GFYNSDGYGG NYNSQGVDWW
     GN
//

If you have problems or comments...

PBIL Back to PBIL home page