DHX9_MOUSE
ID DHX9_MOUSE Reviewed; 1380 AA.
AC O70133; O35931; O54703; Q5FWY1; Q6R5F7; Q9CSA2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=ATP-dependent RNA helicase A {ECO:0000250|UniProtKB:Q08211};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q08211};
DE AltName: Full=DEAH box protein 9 {ECO:0000303|Ref.5};
DE Short=mHEL-5 {ECO:0000303|Ref.5};
DE AltName: Full=Nuclear DNA helicase II {ECO:0000250|UniProtKB:Q08211};
DE Short=NDH II {ECO:0000250|UniProtKB:Q08211};
DE AltName: Full=RNA helicase A {ECO:0000303|PubMed:9480750};
DE Short=RHA {ECO:0000303|PubMed:9480750};
GN Name=Dhx9 {ECO:0000312|MGI:MGI:108177};
GN Synonyms=Ddx9 {ECO:0000250|UniProtKB:Q08211};
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 1-161.
RC STRAIN=129/Sv;
RX PubMed=9480750; DOI=10.1006/geno.1997.5139;
RA Lee C.-G., Eki T., Okumura K., da Costa Soares V., Hurwitz J.;
RT "Molecular analysis of the cDNA and genomic DNA encoding mouse RNA helicase
RT A.";
RL Genomics 47:365-371(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 3).
RC STRAIN=C57BL/6NCr;
RX PubMed=14691545; DOI=10.1371/journal.pbio.0000074;
RA Sharov A.A., Piao Y., Matoba R., Dudekula D.B., Qian Y., VanBuren V.,
RA Falco G., Martin P.R., Stagg C.A., Bassey U.C., Wang Y., Carter M.G.,
RA Hamatani T., Aiba K., Akutsu H., Sharova L., Tanaka T.S., Kimber W.L.,
RA Yoshikawa T., Jaradat S.A., Pantano S., Nagaraja R., Boheler K.R., Taub D.,
RA Hodes R.J., Longo D.L., Schlessinger D., Keller J., Klotz E., Kelsoe G.,
RA Umezawa A., Vescovi A.L., Rossant J., Kunath T., Hogan B.L.M., Curci A.,
RA D'Urso M., Kelso J., Hide W., Ko M.S.H.;
RT "Transcriptome analysis of mouse stem cells and early embryos.";
RL PLoS Biol. 1:410-419(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-264 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE OF 386-919 (ISOFORMS 1/2/3).
RC STRAIN=C57BL/6J;
RA Kisielow P., Miazek A.;
RT "mHEL-5.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10413677; DOI=10.1242/jcs.112.16.2693;
RA Zhang S., Herrmann C., Grosse F.;
RT "Nucleolar localization of murine nuclear DNA helicase II (RNA helicase
RT A).";
RL J. Cell Sci. 112:2693-2703(1999).
RN [7]
RP INTERACTION WITH SP7, AND SUBCELLULAR LOCATION.
RX PubMed=17303075; DOI=10.1016/j.bbrc.2007.01.150;
RA Amorim B.R., Okamura H., Yoshida K., Qiu L., Morimoto H., Haneji T.;
RT "The transcriptional factor Osterix directly interacts with RNA helicase
RT A.";
RL Biochem. Biophys. Res. Commun. 355:347-351(2007).
RN [8]
RP INTERACTION WITH ZIC2.
RX PubMed=17251188; DOI=10.1074/jbc.m610821200;
RA Ishiguro A., Ideta M., Mikoshiba K., Chen D.J., Aruga J.;
RT "ZIC2-dependent transcriptional regulation is mediated by DNA-dependent
RT protein kinase, poly(ADP-ribose) polymerase, and RNA helicase A.";
RL J. Biol. Chem. 282:9983-9995(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EIF2AK2, AND
RP PHOSPHORYLATION.
RX PubMed=19229320; DOI=10.1371/journal.ppat.1000311;
RA Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.;
RT "An antiviral response directed by PKR phosphorylation of the RNA helicase
RT A.";
RL PLoS Pathog. 5:E1000311-E1000311(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-137 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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 [13]
RP FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER COMPLEX.
RX PubMed=22767893; DOI=10.1126/science.1221592;
RA Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.;
RT "Feedback regulation of transcriptional termination by the mammalian
RT circadian clock PERIOD complex.";
RL Science 337:599-602(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, 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 [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1167; ARG-1312; ARG-1323;
RP ARG-1339; ARG-1346; ARG-1353; ARG-1361 AND ARG-1372, AND IDENTIFICATION BY
RP 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 [16]
RP FUNCTION, INTERACTION WITH ADAR, AND ALU RNA-BINDING.
RX PubMed=28355180; DOI=10.1038/nature21715;
RA Aktas T., Avsar Ilik I., Maticzka D., Bhardwaj V., Pessoa Rodrigues C.,
RA Mittler G., Manke T., Backofen R., Akhtar A.;
RT "DHX9 suppresses RNA processing defects originating from the Alu invasion
RT of the human genome.";
RL Nature 544:115-119(2017).
RN [17]
RP FUNCTION.
RX PubMed=28636595; DOI=10.1038/nature22967;
RA Zhu S., Ding S., Wang P., Wei Z., Pan W., Palm N.W., Yang Y., Yu H.,
RA Li H.B., Wang G., Lei X., de Zoete M.R., Zhao J., Zheng Y., Chen H.,
RA Zhao Y., Jurado K.A., Feng N., Shan L., Kluger Y., Lu J., Abraham C.,
RA Fikrig E., Greenberg H.B., Flavell R.A.;
RT "Nlrp9b inflammasome restricts rotavirus infection in intestinal epithelial
RT cells.";
RL Nature 546:667-670(2017).
RN [18]
RP STRUCTURE BY NMR OF 4-262.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of double-stranded RNA-binding motifs from hypothetical
RT protein BAB28848.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [19]
RP INTERACTION WITH ZIC2.
RX PubMed=18068128; DOI=10.1016/j.febslet.2007.11.080;
RA Ishiguro A., Aruga J.;
RT "Functional role of Zic2 phosphorylation in transcriptional regulation.";
RL FEBS Lett. 582:154-158(2008).
CC -!- FUNCTION: Multifunctional ATP-dependent nucleic acid helicase that
CC unwinds DNA and RNA in a 3' to 5' direction and that plays important
CC roles in many processes, such as DNA replication, transcriptional
CC activation, post-transcriptional RNA regulation, mRNA translation and
CC RNA-mediated gene silencing. Requires a 3'-single-stranded tail as
CC entry site for acid nuclei unwinding activities as well as the binding
CC and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide
CC triphosphates (NTPs). Unwinds numerous nucleic acid substrates such as
CC double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks
CC composed of either partially complementary DNA duplexes or DNA:RNA
CC hybrids, respectively, and also DNA and RNA displacement loops (D- and
CC R-loops), triplex-helical DNA (H-DNA) structure and DNA- and RNA-based
CC G-quadruplexes. Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA
CC and poly(A)-containing RNA. Binds also to circular dsDNA or dsRNA of
CC either linear and/or circular forms and stimulates the relaxation of
CC supercoiled DNAs catalyzed by topoisomerase TOP2A. Plays a role in DNA
CC replication at origins of replication and cell cycle progression. Plays
CC a role as a transcriptional coactivator acting as a bridging factor
CC between polymerase II holoenzyme and transcription factors or
CC cofactors, such as BRCA1, CREBBP, RELA and SMN1. Binds to the CDKN2A
CC promoter. Plays several roles in post-transcriptional regulation of
CC gene expression. In cooperation with NUP98, promotes pre-mRNA
CC alternative splicing activities of a subset of genes (By similarity).
CC As component of a large PER complex, is involved in the negative
CC regulation of 3' transcriptional termination of circadian target genes
CC such as PER1 and NR1D1 and the control of the circadian rhythms
CC (PubMed:22767893). Acts also as a nuclear resolvase that is able to
CC bind and neutralize harmful massive secondary double-stranded RNA
CC structures formed by inverted-repeat Alu retrotransposon elements that
CC are inserted and transcribed as parts of genes during the process of
CC gene transposition (PubMed:28355180). Involved in the positive
CC regulation of nuclear export of constitutive transport element (CTE)-
CC containing unspliced mRNA. Component of the coding region determinant
CC (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability.
CC Plays a role in mRNA translation. Positively regulates translation of
CC selected mRNAs through its binding to post-transcriptional control
CC element (PCE) in the 5'-untranslated region (UTR). Involved with LARP6
CC in the translation stimulation of type I collagen mRNAs for CO1A1 and
CC CO1A2 through binding of a specific stem-loop structure in their 5'-
CC UTRs. Stimulates LIN28A-dependent mRNA translation probably by
CC facilitating ribonucleoprotein remodeling during the process of
CC translation. Also plays a role as a small interfering (siRNA)-loading
CC factor involved in the RNA-induced silencing complex (RISC) loading
CC complex (RLC) assembly, and hence functions in the RISC-mediated gene
CC silencing process. Binds preferentially to short double-stranded RNA,
CC such as those produced during rotavirus intestinal infection
CC (PubMed:28636595). This interaction may mediate NLRP9 inflammasome
CC activation and trigger inflammatory response, including IL18 release
CC and pyroptosis (PubMed:28636595). Finally, mediates the attachment of
CC heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in
CC the nucleus (By similarity). {ECO:0000250|UniProtKB:Q08211,
CC ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:28355180,
CC ECO:0000269|PubMed:28636595}.
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 Evidence={ECO:0000250|UniProtKB:Q08211};
CC -!- SUBUNIT: Component of the coding region determinant (CRD)-mediated
CC complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1.
CC Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1,
CC HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing
CC untranslated mRNAs (By similarity). The large PER complex involved in
CC the repression of transcriptional termination is composed of at least
CC PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (PubMed:22767893).
CC Associates (via DRBM domains) with the RISC complex; this association
CC occurs in a small interfering (siRNA)-dependent manner. Associates with
CC the SMN complex; this association induces recruitment of DHX9 to the
CC RNA polymerase II. Associates with polysomes in a LIN28A-dependent
CC manner. Interacts (via C-terminus) with ACTB; this interaction is
CC direct and mediates the attachment to nuclear ribonucleoprotein
CC complexes (By similarity). Interacts with ADAR isoform 1; this
CC interaction occurs in a RNA-independent manner (PubMed:28355180).
CC Interacts (via DRBM domains) with AGO2 (via middle region); this
CC interaction promotes active RISC assembly by promoting the association
CC of siRNA with AGO2. Interacts (via NTD domain) with AKAP8L (via N-
CC terminus). Interacts with BRCA1 (via C-terminus); this interaction is
CC direct and links BRCA1 to the RNA polymerase II holoenzyme. Interacts
CC (via N-terminus) with CREBBP; this interaction mediates association
CC with RNA polymerase II holoenzyme and stimulates CREB-dependent
CC transcriptional activation (By similarity). Interacts (via N-terminus)
CC with EIF2AK2/PKR; this interaction is dependent upon the activation of
CC the kinase (PubMed:19229320). Interacts (via DRBM domains) with DICER1.
CC Interacts with H2AX; this interaction is direct, requires
CC phosphorylation of histone H2AX on 'Ser-140' by PRKDC and promotes
CC binding of DHX9 to transcriptionally stalled sites on chromosomal DNA
CC in response to genotoxic stress. Interacts with HNRNPC; this
CC interaction is direct, enhanced probably by their concomitant binding
CC to RNA and mediates the attachment to actin filaments. Interacts (via
CC NTD domain) with PRMT1. Interacts with IGF2BP1. Interacts with IGF2BP2,
CC IGF2BP3. Interacts (via DRBM domains) with ILF3; this interaction
CC occurs in a RNA-independent manner. Interacts with Importin
CC alpha/Importin beta receptor. Interacts with LARP6 (via C-terminus);
CC this interaction occurs in a mRNA-independent manner. Interacts (via
CC N- and C-terminus) with LIN28A (via C-terminus); this interaction
CC occurs in a RNA-independent manner. Interacts with LMX1B. Interacts
CC (via helicase C-terminal domain, HA2 and OB-fold regions) with MAVS
CC (via CARD domain); this interaction occurs in both resting and double-
CC stranded RNA poly(I:C)-induced cells. Interacts with MBD2; this
CC interaction stimulates transcriptional activation in a CREB-dependent
CC manner. Interacts (via H2A and OB-fold regions) with MYD88 (via TIR
CC domain); this interaction is direct. Interacts with NLRP9 upon
CC rotavirus infection; this interaction may trigger NLRP9 inflammasome
CC activation and inflammatory response. Interacts (via DRBM, OB-fold and
CC RGG regions) with NUP98 (via N-terminus); this interaction occurs in a
CC RNA-dependent manner and stimulates DHX9-mediated ATPase activity and
CC regulates transcription and splicing of a subset of genes. Interacts
CC (via N-terminus) with NXF1 (via N-terminus); this interaction is direct
CC and negatively regulates NXF1-mediated nuclear export of constitutive
CC transport element (CTE)-containing cellular mRNAs. Interacts with RELA;
CC this interaction is direct and activates NF-kappa-B-mediated
CC transcription. Interacts (via MTAD region) with RNA polymerase II
CC holoenzyme; this interaction stimulates transcription activation in a
CC CREB-dependent manner. Interacts (via RGG region) with SMN1; this
CC interaction links SMN1 to the RNA polymerase II holoenzyme (By
CC similarity). Interacts with SP7 (PubMed:17303075). Interacts (via DRBM
CC domains) with TARBP2 (via DRBM first and second domains); this
CC interaction occurs in a small interfering (siRNA)-dependent manner.
CC Interacts with TOP2A; this interaction occurs in a E2 enzyme UBE2I- and
CC RNA-dependent manner, negatively regulates DHX9-mediated double-
CC stranded DNA and RNA duplex helicase activity and stimulates TOP2A-
CC mediated supercoiled DNA relaxation activity. Interacts (via DRBM
CC domains and C-terminus) with WRN (via 3'-5' exonuclease domain); this
CC interaction inhibits the DNA-dependent NTPase and DNA helicase
CC activities of DHX9 and stimulates the 3'-5' exonuclease activity of
CC WRN. Interacts with XRCC5; this interaction occurs in a RNA-dependent
CC manner (By similarity). Interacts with ZIC2 (via C2H2-type domain 3)
CC (PubMed:17251188). Interacts with MCM3AP (By similarity).
CC {ECO:0000250|UniProtKB:Q08211, ECO:0000269|PubMed:17251188,
CC ECO:0000269|PubMed:17303075, ECO:0000269|PubMed:19229320,
CC ECO:0000269|PubMed:22767893, ECO:0000269|PubMed:28355180}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17303075}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q08211}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:10413677}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q08211}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q08211}.
CC Note=Nucleoplasmic shuttling protein. Its nuclear import involves the
CC nucleocytoplasmic transport receptor Importin alpha/Importin beta
CC receptor pathway in a Ran-dependent manner. In interphase, localizes in
CC nuclear stress granules and at perichromatin fibrils and in cytoplasmic
CC ribonucleoprotein granules. Colocalizes with WRN and H2AX at
CC centrosomes in a microtubule-dependent manner following DNA damaging
CC agent treatment. Excluded from the mitotic nucleus as early as prophase
CC and re-entered the nucleus at telophase. Recruited in diffuse and
CC discrete intranuclear foci (GLFG-body) in a NUP98-dependent manner (By
CC similarity). Colocalizes with SP7 in the nucleus (PubMed:17303075).
CC Colocalizes with ACTB at nuclear actin filaments inside the nucleus or
CC at the nuclear pore. Colocalizes with HNRNPC at nuclear
CC ribonucleoprotein complex proteins in the nucleus. Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs (By
CC similarity). {ECO:0000250|UniProtKB:Q08211,
CC ECO:0000269|PubMed:17303075}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O70133-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O70133-2; Sequence=VSP_014779;
CC Name=3;
CC IsoId=O70133-3; Sequence=VSP_014778;
CC -!- DOMAIN: DRBM domains cooperate for the binding to nucleic acid but not
CC for unwinding helicase activity. The helicase-associated domain-2 (HA2)
CC region is essential for the duplex RNA unwinding helicase activity. The
CC minimal transactivation region (MTAD) mediates interaction with the RNA
CC polymerase II holoenzyme and stimulates transcriptional activation in a
CC CREB-dependent manner. The oligonucleotide- or oligosaccharide-binding
CC (OB-fold) and the repeated arginine and glycine-glycine (RGG) regions
CC are dispensable for both RNA-binding and unwinding helicase activities.
CC The RGG region contains both nuclear localization signal (NLS) and
CC nuclear export signal (NES) and is necessary and sufficient for
CC nucleocytoplasmic shuttling in a RNA-independent manner.
CC {ECO:0000250|UniProtKB:Q08211}.
CC -!- PTM: Methylated. PRMT1-mediated methylation of undefined Arg residues
CC in the nuclear transport domain (NTD) is required for nuclear import of
CC DHX9. {ECO:0000250|UniProtKB:Q08211}.
CC -!- PTM: Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent
CC manner. Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its
CC association with double-stranded RNA. {ECO:0000250|UniProtKB:Q08211}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH89159.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAR87796.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; U91922; AAC05725.1; -; mRNA.
DR EMBL; AF023530; AAC05301.1; -; Genomic_DNA.
DR EMBL; AY512925; AAR87796.1; ALT_SEQ; mRNA.
DR EMBL; BC089159; AAH89159.1; ALT_SEQ; mRNA.
DR EMBL; AK013423; BAB28848.1; -; mRNA.
DR EMBL; U92080; AAB72087.1; -; mRNA.
DR RefSeq; NP_031868.2; NM_007842.2.
DR PDB; 1UIL; NMR; -; A=163-262.
DR PDB; 1WHQ; NMR; -; A=4-89.
DR PDB; 2RS6; NMR; -; A=4-89.
DR PDB; 2RS7; NMR; -; A=163-262.
DR PDBsum; 1UIL; -.
DR PDBsum; 1WHQ; -.
DR PDBsum; 2RS6; -.
DR PDBsum; 2RS7; -.
DR AlphaFoldDB; O70133; -.
DR BMRB; O70133; -.
DR SMR; O70133; -.
DR BioGRID; 199088; 104.
DR ComplexPortal; CPX-1089; CRD-mediated mRNA stability complex.
DR IntAct; O70133; 17.
DR MINT; O70133; -.
DR STRING; 10090.ENSMUSP00000038135; -.
DR iPTMnet; O70133; -.
DR PhosphoSitePlus; O70133; -.
DR SwissPalm; O70133; -.
DR EPD; O70133; -.
DR jPOST; O70133; -.
DR MaxQB; O70133; -.
DR PaxDb; O70133; -.
DR PeptideAtlas; O70133; -.
DR PRIDE; O70133; -.
DR ProteomicsDB; 279535; -. [O70133-1]
DR ProteomicsDB; 279536; -. [O70133-2]
DR ProteomicsDB; 279537; -. [O70133-3]
DR DNASU; 13211; -.
DR GeneID; 13211; -.
DR KEGG; mmu:13211; -.
DR CTD; 1660; -.
DR MGI; MGI:108177; Dhx9.
DR eggNOG; KOG0921; Eukaryota.
DR InParanoid; O70133; -.
DR PhylomeDB; O70133; -.
DR BRENDA; 3.6.4.13; 3474.
DR Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 13211; 22 hits in 55 CRISPR screens.
DR ChiTaRS; Dhx9; mouse.
DR EvolutionaryTrace; O70133; -.
DR PRO; PR:O70133; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70133; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005726; C:perichromatin fibrils; ISS:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0016442; C:RISC complex; ISS:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0033679; F:3'-5' DNA/RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
DR GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0001069; F:regulatory region RNA binding; IDA:UniProtKB.
DR GO; GO:1905172; F:RISC complex 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:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0035197; F:siRNA binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0045142; F:triplex DNA binding; ISS:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IMP:MGI.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0039695; P:DNA-templated viral transcription; ISO:MGI.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:UniProtKB.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0032741; P:positive regulation of interleukin-18 production; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1905698; P:positive regulation of polysome binding; ISS:UniProtKB.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0050434; P:positive regulation of viral transcription; ISO:MGI.
DR GO; GO:1904973; P:positive regulation of viral translation; ISO:MGI.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0070269; P:pyroptosis; IMP:UniProtKB.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0050691; P:regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0070922; P:RISC complex assembly; ISS:UniProtKB.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
DR CDD; cd17972; DEXHc_DHX9; 1.
DR CDD; cd19854; DSRM_DHX9_rpt1; 1.
DR CDD; cd19855; DSRM_DHX9_rpt2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044447; DHX9_DEXHc.
DR InterPro; IPR044445; DHX9_DSRM_1.
DR InterPro; IPR044446; DHX9_DSRM_2.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding;
KW Biological rhythms; Cytoplasm; Cytoskeleton; DNA-binding; Helicase;
KW Hydrolase; Immunity; Inflammatory response; Innate immunity;
KW Isopeptide bond; Manganese; Metal-binding; Methylation; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW Transcription; Transcription regulation; Transcription termination;
KW Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..1380
FT /note="ATP-dependent RNA helicase A"
FT /id="PRO_0000055158"
FT DOMAIN 3..71
FT /note="DRBM 1"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 182..254
FT /note="DRBM 2"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 400..566
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 638..811
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..252
FT /note="Interaction with CREBBP"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 5..9
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 53..55
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 87..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..188
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 232..327
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 236..238
FT /note="siRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 257..666
FT /note="Necessary for interaction with RNA polymerase II
FT holoenzyme"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 315..954
FT /note="Necessary for interaction with H2AX"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 333..382
FT /note="MTAD"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 400..811
FT /note="Core helicase"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 588..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..921
FT /note="HA2"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 960..1076
FT /note="OB-fold"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 1151..1366
FT /note="NTD region"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT REGION 1152..1380
FT /note="RGG"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOTIF 513..516
FT /note="DEAH box"
FT MOTIF 588..597
FT /note="Nuclear localization signal (NLS1)"
FT /evidence="ECO:0000255"
FT MOTIF 1156..1174
FT /note="Nuclear localization signal (NLS2)"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT BINDING 413..421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08211,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT BINDING 514
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 148
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 148
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 201
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1026
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1167
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1176
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT MOD_RES 1312
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1323
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1339
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1346
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1353
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1361
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1372
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08211"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14691545"
FT /id="VSP_014778"
FT VAR_SEQ 123
FT /note="E -> EA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014779"
FT CONFLICT 46
FT /note="A -> R (in Ref. 1; AAC05725)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="S -> A (in Ref. 1; AAC05725/AAC05301)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="L -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="Q -> H (in Ref. 1; AAC05725)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="R -> G (in Ref. 4; BAB28848)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="S -> C (in Ref. 1; AAC05725)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="V -> C (in Ref. 1; AAC05725)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="S -> P (in Ref. 1; AAC05725)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="N -> M (in Ref. 5; AAB72087)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="T -> I (in Ref. 5; AAB72087)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="I -> V (in Ref. 5; AAB72087)"
FT /evidence="ECO:0000305"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:1WHQ"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:1WHQ"
FT STRAND 29..39
FT /evidence="ECO:0007829|PDB:1WHQ"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1WHQ"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:1WHQ"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1WHQ"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1UIL"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:1UIL"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:1UIL"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:1UIL"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:1UIL"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1UIL"
FT HELIX 237..255
FT /evidence="ECO:0007829|PDB:1UIL"
FT MOD_RES O70133-2:137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1380 AA; 149475 MW; 005D641CD9A4F0C9 CRC64;
MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN STNKKDAQSN
AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA SAAEGLPAPM GGPLPPHLAL
KAEENNSGVE SSGYGSPGPT WDRGANLKDY YSRKEEQEVQ ATLESEEVDL NAGLHGNWTL
ENAKARLNQY FQKEKIQGEY KYTQVGPDHN RSFIAEMTIY IKQLGRRIFA REHGSNKKLA
AQSCALSLVR QLYHLGVIEA YSGLTKKKEG ERVEPYKVFL SPDLELQLQN VVQELDLEIV
PPPVDPSMPV ILNIGKLAHF EPSQRQNAVG VVPWSPPQSN WNPWTSSNID EGPLAYASTE
QISMDLKNEL TYQMEQDHNL QSVLQERELL PVKKFEAEIL EAISSNSVVI IRGATGCGKT
TQVPQYILDD FIQNDRAAEC NIVVTQPRRI SAVAVAERVA YERGEEPGKS CGYSVRFESI
LPRPHASIMF CTVGVLLRKL EAGIRGISHV IVDEIHERDI NTDFLLVVLR DVVLAYPEVR
IVLMSATIDT TMFCEYFFNC PIIEVYGRTF PVQEYFLEDC IQMTQFIPPP KDKKKKDKED
DGGEDDDANC NLICGDEYGP ETKLSMSQLN EKETPFELIE ALLKYIETLN VPGAVLVFLP
GWNLIYTMQK HLENNSHFGS HRYQILPLHS QIPREEQRKV FDPVPDGVTK VILSTNIAET
SITINDVVYV IDSCKQKVKL FTAHNNMTNY ATVWASKTNL EQRKGRAGRV RPGFCFHLCS
RARFDRLETH MTPEMFRTPL HEIALSIKLL RLGGIGQFLA KAIEPPPLDA IIEAEHTLRE
LDALDANDEL TPLGRILAKL PIEPRFGKMM IMGCIFYVGD AVCTISAATC FPEPFISEGK
RLGYIHRNFA GNRFSDHVAL LSVFQAWDDA RMSGEEAEIR FCEQKRLNMA TLRMTWEAKV
QLKEILINSG FPEDCLLTQV FTNTGPDNNL DVVISLLAFG VYPNVCYHKE KRKILTTEGR
NALIHKSSVN CPFSSQDMKY PSPFFVFGEK IRTRAISAKG MTLVTPLQLL LFASKKVQSD
GQIVFIDDWI RLQISHEAAA CITIRAAMEA LVVEVSKQPN IISQLDPVNE HMLNTIRQIS
RPSAAGINLM IGSVRYGDGP RPPKMARYDN GSGYRRGYGG GGYGGGGYGG GYGSGGFGGG
FGSGGGFGGG FNSGGGGFGS GGGGFGSGGG GFGGGGGGFS GGGGGGFGGG RGGGGGGFGG
SGGFGNGGGG YGVGGGGYGG GGGGGYGGGS GGYGGGGYGG GEGYSISPNS YRGNYGGGGG
GYRGGSQGGY RNNFGGDYRG SSGDYRGSGG GYRGSGGFQR RGYGGGYFGQ GRGGGGGGGY
