DDX17_MOUSE
ID DDX17_MOUSE Reviewed; 650 AA.
AC Q501J6; Q6P5G1; Q8BIN2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX17;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 17;
GN Name=Ddx17;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [3]
RP FUNCTION, AND INTERACTION WITH MYOD1.
RX PubMed=17011493; DOI=10.1016/j.devcel.2006.08.003;
RA Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P., Ogryzko V.,
RA Fuller-Pace F.V., Hoffman E.P., Tapscott S.J., Sartorelli V.;
RT "The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators of
RT MyoD and skeletal muscle differentiation.";
RL Dev. Cell 11:547-560(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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 [5]
RP FUNCTION IN ALTERNATIVE SPLICING.
RX PubMed=23022728; DOI=10.1038/nsmb.2390;
RA Dardenne E., Pierredon S., Driouch K., Gratadou L., Lacroix-Triki M.,
RA Espinoza M.P., Zonta E., Germann S., Mortada H., Villemin J.P.,
RA Dutertre M., Lidereau R., Vagner S., Auboeuf D.;
RT "Splicing switch of an epigenetic regulator by RNA helicases promotes
RT tumor-cell invasiveness.";
RL Nat. Struct. Mol. Biol. 19:1139-1146(2012).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-605, AND IDENTIFICATION BY MASS
RP 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 [7]
RP FUNCTION.
RX PubMed=26947125; DOI=10.1038/srep22848;
RA Remenyi J., Bajan S., Fuller-Pace F.V., Arthur J.S., Hutvagner G.;
RT "The loop structure and the RNA helicase p72/DDX17 influence the processing
RT efficiency of the mice miR-132.";
RL Sci. Rep. 6:22848-22848(2016).
CC -!- FUNCTION: As an RNA helicase, unwinds RNA and alters RNA structures
CC through ATP binding and hydrolysis. Involved in multiple cellular
CC processes, including pre-mRNA splicing, alternative splicing, ribosomal
CC RNA processing and miRNA processing, as well as transcription
CC regulation. Regulates the alternative splicing of exons exhibiting
CC specific features. This function requires the RNA helicase activity.
CC Affects NFAT5 and histone macro-H2A.1/MACROH2A1 alternative splicing in
CC a CDK9-dependent manner. Affects splicing of mediators of steroid
CC hormone signaling pathway, including kinases that phosphorylates ESR1
CC and transcriptional regulators. By acting splicing of regulatory
CC factors, participates in ESR1 and AR stabilization. Promotes the
CC inclusion of specific AC-rich alternative exons in CD44 transcripts. In
CC myoblasts and epithelial cells, cooperates with HNRNPH1 to control the
CC splicing of specific subsets of exons. In addition to binding mature
CC mRNAs, also interacts with certain pri-microRNAs, including MIR132/miR-
CC 132, and stabilizes the primary transcript. Also participates in the
CC MIR132 processing, resulting in significantly higher levels of mature
CC MIR132 than MIR212 despite the fact that both are cotranscribed and co-
CC regulated (PubMed:26947125). Binding of pri-microRNAs may occur on the
CC 3' segment flanking the stem loop via the 5'-[ACG]CAUC[ACU]-3'
CC consensus sequence (By similarity). Participates in MYC down-regulation
CC at high cell density through the production of MYC-targeting microRNAs.
CC Along with DDX5, may be involved in the processing of the 32S
CC intermediate into the mature 28S rRNA. Promoter-specific transcription
CC regulator, functioning as a coactivator or corepressor depending on the
CC context of the promoter and the transcriptional complex in which it
CC exists. Enhances NFAT5 transcriptional activity. Synergizes with TP53
CC in the activation of the MDM2 promoter; this activity requires
CC acetylation on lysine residues. May also coactivate MDM2 transcription
CC through a TP53-independent pathway. Coactivates MMP7 transcription.
CC Along with CTNNB1, coactivates MYC, JUN, FOSL1 and cyclin D1/CCND1
CC transcription. Alone or in combination with DDX5 and/or SRA1 non-coding
CC RNA, plays a critical role in promoting the assembly of proteins
CC required for the formation of the transcription initiation complex and
CC chromatin remodeling leading to coactivation of MYOD1-dependent
CC transcription. This helicase-independent activity is required for
CC skeletal muscle cells to properly differentiate into myotubes
CC (PubMed:17011493). During epithelial-to-mesenchymal transition,
CC coregulates SMAD-dependent transcriptional activity, directly
CC controlling key effectors of differentiation, including miRNAs which in
CC turn directly repress its expression. Plays a role in estrogen and
CC testosterone signaling pathway at several levels. Mediates the use of
CC alternative promoters in estrogen-responsive genes and regulates
CC transcription and splicing of a large number of steroid hormone target
CC genes. Contrary to the splicing regulation activity, transcriptional
CC coregulation of the estrogen receptor ESR1 is helicase activity-
CC independent. Plays a role in innate immunity. Specifically restricts
CC bunyavirus infection, including Rift Valley fever virus (RVFV) or La
CC Crosse virus (LACV), but not vesicular stomatitis virus (VSV), in an
CC interferon- and DROSHA-independent manner. Binds to RVFV RNA, likely
CC via structured viral RNA elements (By similarity). Promotes mRNA
CC degradation mediated by the antiviral zinc-finger protein ZC3HAV1, in
CC an ATPase-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q92841, ECO:0000269|PubMed:17011493,
CC ECO:0000269|PubMed:26947125}.
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:Q92841};
CC -!- SUBUNIT: Interacts with DDX5 in an RNA-independent manner (By
CC similarity). Interacts with CDK9 transcription elongation complex under
CC basal conditions. Following cell stimulation with poly(I:C), a
CC synthetic double-stranded RNA mimicking viral infection, the
CC interaction with CDK9 is decreased (By similarity). Interacts with ESR1
CC in an estrogen-independent manner (By similarity). Interacts with
CC HNRNPH1; this interaction is important for the regulation of
CC alternative splicing on G-quadruplex structures (By similarity). At
CC high, but not low, cell density, interacts with DROSHA and DGCR8, the
CC core components of the microprocessor complex involved in the
CC maturation of primary microRNAs (pri-miRNAs) into pre-miRNAs. The
CC interaction with DGCR8 is reduced during mitosis. At low, but not high,
CC cell density, interacts with YAP1 and with its paralog, WWTR1/TAZ.
CC Interactions with DROSHA and YAP1 are mutually exclusive. In vitro, the
CC pre-miRNA processing activity of the DDX17-containing microprocessor
CC complex is weaker than that of the DROSHA/DGCR8 microprocessor complex
CC (By similarity). Interacts with UPF3B (By similarity). Interacts with
CC NFAT5; this interaction leads to DDX17 recruitment to LNC2 and S100A4
CC promoters and NFAT5-mediated DDX17-enhanced transactivation (By
CC similarity). Interacts with HDAC1, HDAC2 and HDAC3; this interaction
CC with HDAC1 and HDAC3, but not HDAC2, depends upon DDX17 acetylation (By
CC similarity). Interacts with ZC3HAV1 (via N-terminal domain) in an RNA-
CC independent manner. Interacts with EXOSC3/RRP40 and EXOSC5/RRP46; this
CC interaction may be indirect and mediated by ZC3HAV1-binding (By
CC similarity). Interacts with EP300; this interaction leads to
CC acetylation at lysine residues (By similarity). Interacts with
CC CREBBP/CBP and KAT2B/P/CAF (By similarity). Directly interacts with
CC CTNNB1 (By similarity). Interacts with MYOD1 (PubMed:17011493).
CC Interacts with TP53 (By similarity). Interacts with DCP1A in an RNA-
CC independent manner. Interacts with DCP2 in an RNA-dependent manner (By
CC similarity). Interacts with DHX36; this interaction occurs in a RNA-
CC dependent manner (By similarity). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:Q92841, ECO:0000269|PubMed:17011493}.
CC -!- INTERACTION:
CC Q501J6; P46938: Yap1; NbExp=3; IntAct=EBI-911206, EBI-1211949;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92841}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q92841}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q92841}. Note=In the course of bunyavirus
CC infection, relocalizes from the nucleus to the cytosol where it binds
CC viral RNA to antagonize replication. {ECO:0000250|UniProtKB:Q92841}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q501J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q501J6-2; Sequence=VSP_015780, VSP_015781;
CC -!- PTM: Sumoylation significantly increases stability. It also promotes
CC interaction specifically with HDAC1 (but not HDAC2, nor HDAC3) and
CC strongly stimulates ESR1 and TP53 coactivation.
CC {ECO:0000250|UniProtKB:Q92841}.
CC -!- PTM: Acetylation at lysine residues stabilizes the protein, stimulates
CC interaction with HDAC1 and HDAC3, but not HDAC2, and represses ESR1 and
CC TP53 coactivation activity. {ECO:0000250|UniProtKB:Q92841}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; AK039888; BAC30474.1; -; mRNA.
DR EMBL; BC062910; AAH62910.1; -; mRNA.
DR EMBL; BC096036; AAH96036.1; -; mRNA.
DR CCDS; CCDS88804.1; -. [Q501J6-2]
DR CCDS; CCDS88805.1; -. [Q501J6-1]
DR RefSeq; NP_001035277.1; NM_001040187.1. [Q501J6-1]
DR RefSeq; NP_951061.1; NM_199079.1. [Q501J6-2]
DR RefSeq; NP_951062.1; NM_199080.2.
DR AlphaFoldDB; Q501J6; -.
DR SMR; Q501J6; -.
DR BioGRID; 211894; 54.
DR CORUM; Q501J6; -.
DR IntAct; Q501J6; 11.
DR MINT; Q501J6; -.
DR STRING; 10090.ENSMUSP00000055535; -.
DR iPTMnet; Q501J6; -.
DR PhosphoSitePlus; Q501J6; -.
DR SwissPalm; Q501J6; -.
DR REPRODUCTION-2DPAGE; IPI00405364; -.
DR EPD; Q501J6; -.
DR jPOST; Q501J6; -.
DR MaxQB; Q501J6; -.
DR PaxDb; Q501J6; -.
DR PeptideAtlas; Q501J6; -.
DR PRIDE; Q501J6; -.
DR ProteomicsDB; 279898; -. [Q501J6-1]
DR ProteomicsDB; 279899; -. [Q501J6-2]
DR Antibodypedia; 26352; 248 antibodies from 29 providers.
DR DNASU; 67040; -.
DR Ensembl; ENSMUST00000229431; ENSMUSP00000155737; ENSMUSG00000055065. [Q501J6-2]
DR Ensembl; ENSMUST00000229877; ENSMUSP00000155307; ENSMUSG00000055065. [Q501J6-1]
DR GeneID; 67040; -.
DR KEGG; mmu:67040; -.
DR UCSC; uc007wtq.1; mouse. [Q501J6-1]
DR UCSC; uc007wtt.1; mouse. [Q501J6-2]
DR CTD; 10521; -.
DR MGI; MGI:1914290; Ddx17.
DR VEuPathDB; HostDB:ENSMUSG00000055065; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000160049; -.
DR InParanoid; Q501J6; -.
DR OrthoDB; 638613at2759; -.
DR BRENDA; 3.6.4.13; 3474.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR BioGRID-ORCS; 67040; 6 hits in 78 CRISPR screens.
DR ChiTaRS; Ddx17; mouse.
DR PRO; PR:Q501J6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q501J6; protein.
DR Bgee; ENSMUSG00000055065; Expressed in renal medulla collecting duct and 262 other tissues.
DR ExpressionAtlas; Q501J6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0106222; F:lncRNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0061614; P:miRNA transcription; IMP:UniProtKB.
DR GO; GO:0045445; P:myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd18050; DEADc_DDX17; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR046330; DDX17_ATP-bd-dom.
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;
KW Acetylation; Alternative splicing; Antiviral defense; ATP-binding;
KW Cytoplasm; Helicase; Hydrolase; Immunity; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; rRNA processing; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..650
FT /note="Probable ATP-dependent RNA helicase DDX17"
FT /id="PRO_0000054994"
FT DOMAIN 123..298
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 326..473
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..650
FT /note="Transactivation domain"
FT /evidence="ECO:0000250"
FT REGION 472..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..647
FT /note="Interaction with YAP1"
FT /evidence="ECO:0000250|UniProtKB:Q92841"
FT MOTIF 92..120
FT /note="Q motif"
FT MOTIF 246..249
FT /note="DEAD box"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92841"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92841"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92841"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92841"
FT MOD_RES 605
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92841"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92841"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92841"
FT VAR_SEQ 404..407
FT /note="DVED -> GLYR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015780"
FT VAR_SEQ 408..650
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015781"
FT CONFLICT 320
FT /note="E -> V (in Ref. 2; AAH62910)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="D -> Y (in Ref. 2; AAH62910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 72399 MW; E2590F3E53883D3C CRC64;
MRGGGFGDRD RDRDRGGFGA RGGSGLPPKK FGNPGERLRK KKWDLSELPK FEKNFYVEHP
EVARLTPYEV DELRRKKEIT VRGGDVCPKP VFAFHHANFP QYVMDVLMDQ HFTEPTPIQC
QGFPLALSGR DMVGIAQTGS GKTLAYLLPA IVHINHQPYL ERGDGPICLV LAPTRELAQQ
VQQVADDYGK CSRLKSTCIY GGAPKGPQIR DLERGVEICI ATPGRLIDFL ESGKTNLRRC
TYLVLDEADR MLDMGFEPQI RKIVDQIRPD RQTLMWSATW PKEVRQLAED FLRDYTQINV
GNLELSANHN ILQIVDVCME SEKDHKLIQL MEEIMAEKEN KTIIFVETKR RCDDLTRRMR
RDGWPAMCIH GDKSQPERDW VLNEFRSGKA PILIATDVAS RGLDVEDVKF VINYDYPNSS
EDYVHRIGRT ARSTNKGTAY TFFTPGNLKQ ARELIKVLEE ANQAINPKLM QLVDHRGGGG
GGGGRSRYRT TSSANNPNLM YQDECDRRLR GVKDGGRRDS TSYRDRSETD RASYANGSGY
GSPNSAFGAQ AGQYTYAQGT YGAAAYGTSG YTAQEYAAGT YGASSTASAG RSSQSSSQQF
SGIGRSGQQP QPLMSQQFAQ PPGATNMIGY MGQTAYQYPP PPPPPPPSRK
