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 24-JAN-2024, entry version 157. 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, 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 [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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 56. DR CORUM; Q501J6; -. DR IntAct; Q501J6; 11. DR MINT; Q501J6; -. DR STRING; 10090.ENSMUSP00000055535; -. DR GlyGen; Q501J6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q501J6; -. DR PhosphoSitePlus; Q501J6; -. DR SwissPalm; Q501J6; -. DR REPRODUCTION-2DPAGE; IPI00405364; -. DR EPD; Q501J6; -. DR jPOST; Q501J6; -. DR MaxQB; Q501J6; -. DR PaxDb; 10090-ENSMUSP00000055535; -. DR PeptideAtlas; Q501J6; -. DR ProteomicsDB; 279898; -. [Q501J6-1] DR ProteomicsDB; 279899; -. [Q501J6-2] DR Pumba; Q501J6; -. DR Antibodypedia; 26352; 278 antibodies from 29 providers. DR DNASU; 67040; -. DR Ensembl; ENSMUST00000229431.2; ENSMUSP00000155737.2; ENSMUSG00000055065.8. [Q501J6-2] DR Ensembl; ENSMUST00000229877.2; ENSMUSP00000155307.2; ENSMUSG00000055065.8. [Q501J6-1] DR GeneID; 67040; -. DR KEGG; mmu:67040; -. DR UCSC; uc007wtq.1; mouse. [Q501J6-1] DR UCSC; uc007wtt.1; mouse. [Q501J6-2] DR AGR; MGI:1914290; -. DR CTD; 10521; -. DR MGI; MGI:1914290; Ddx17. DR VEuPathDB; HostDB:ENSMUSG00000055065; -. DR eggNOG; KOG0331; Eukaryota. DR GeneTree; ENSGT00940000160049; -. DR InParanoid; Q501J6; -. DR OrthoDB; 5477821at2759; -. DR BRENDA; 3.6.4.13; 3474. DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors. DR BioGRID-ORCS; 67040; 6 hits in 84 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 266 other cell types or tissues. DR ExpressionAtlas; Q501J6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central. DR GO; GO:0043021; F:ribonucleoprotein complex 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: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:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR CDD; cd18050; DEADc_DDX17; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1. DR PANTHER; PTHR47958:SF140; ATP-DEPENDENT RNA HELICASE DDX17-RELATED; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 //