ID HLTF_HUMAN Reviewed; 1009 AA. AC Q14527; D3DNH3; Q14536; Q16051; Q7KYJ6; Q86YA5; Q92652; Q96KM9; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 2. DT 13-SEP-2023, entry version 207. DE RecName: Full=Helicase-like transcription factor; DE EC=2.3.2.27; DE EC=3.6.4.-; DE AltName: Full=DNA-binding protein/plasminogen activator inhibitor 1 regulator; DE AltName: Full=HIP116; DE AltName: Full=RING finger protein 80; DE AltName: Full=RING-type E3 ubiquitin transferase HLTF {ECO:0000305}; DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3; DE AltName: Full=Sucrose nonfermenting protein 2-like 3; GN Name=HLTF; Synonyms=HIP116A, RNF80, SMARCA3, SNF2L3, ZBU1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Cervix carcinoma; RX PubMed=7876228; DOI=10.1074/jbc.270.9.4575; RA Sheridan P.L., Schorpp M., Voz M.L., Jones K.A.; RT "Cloning of an SNF2/SWI2-related protein that binds specifically to the SPH RT motifs of the SV40 enhancer and to the HIV-1 promoter."; RL J. Biol. Chem. 270:4575-4587(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ALTERNATIVE RP INITIATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=8672239; DOI=10.1089/dna.1996.15.429; RA Ding H., Descheemaeker K., Marynen P., Nelles L., Carvalho T., RA Carmo-Fonseca M., Collen D., Belayew A.; RT "Characterization of a helicase-like transcription factor involved in the RT expression of the human plasminogen activator inhibitor-1 gene."; RL DNA Cell Biol. 15:429-442(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Ribaucour F., Wiedig M., Benotmane A.M., Coppee F., Belayew A.; RT "Characterization of the human SMARCA3/HLTF gene."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-213. RX PubMed=8342330; RA Descheemaeker K.; RT "On the regulation of the plasminogen activator inhibitor-1 gene RT expression."; RL Verh. K. Acad. Geneeskd. Belg. 55:225-264(1993). RN [7] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=9126292; DOI=10.1006/dbio.1996.8486; RA Gong X., Kaushal S., Ceccarelli E., Bogdanova N., Neville C., Nguyen T., RA Clark H., Khatib Z.A., Valentine M., Look A.T., Rosenthal N.; RT "Developmental regulation of Zbu1, a DNA-binding member of the SWI2/SNF2 RT family."; RL Dev. Biol. 183:166-182(1997). RN [8] RP FUNCTION, AND INTERACTION WITH SP1 AND SP3. RX PubMed=10391891; DOI=10.1074/jbc.274.28.19573; RA Ding H., Benotmane A.M., Suske G., Collen D., Belayew A.; RT "Functional interactions between Sp1 or Sp3 and the helicase-like RT transcription factor mediate basal expression from the human plasminogen RT activator inhibitor-1 gene."; RL J. Biol. Chem. 274:19573-19580(1999). RN [9] RP EPIGENETIC INACTIVATION IN COLON CANCER. RX PubMed=11904375; DOI=10.1073/pnas.062459899; RA Moinova H.R., Chen W.-D., Shen L., Smiraglia D., Olechnowicz J., Ravi L., RA Kasturi L., Myeroff L., Plass C., Parsons R., Minna J., Willson J.K.V., RA Green S.B., Issa J.-P., Markowitz S.D.; RT "HLTF gene silencing in human colon cancer."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4562-4567(2002). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-398; SER-400 AND RP THR-736, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH PCNA; RP UBE2N AND RAD18. RX PubMed=18316726; DOI=10.1073/pnas.0800563105; RA Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., RA Prakash S., Haracska L.; RT "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear RT antigen polyubiquitination."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008). RN [13] RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH PCNA; RP RAD18; SHPRH AND UBE2N. RX PubMed=18719106; DOI=10.1073/pnas.0805685105; RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., RA Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.; RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH RT prevents genomic instability from stalled replication forks."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP PHOSPHORYLATION AT TYR-195. RX PubMed=21457752; DOI=10.1016/j.mce.2011.03.009; RA Helmer R.A., Dertien J.S., Chilton B.S.; RT "Prolactin induces Jak2 phosphorylation of RUSHY195."; RL Mol. Cell. Endocrinol. 338:79-83(2011). RN [18] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-27, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-211, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [20] RP STRUCTURE BY NMR OF 51-171. RG Structural genomics consortium (SGC); RT "NMR structure of the HLTF hiran domain."; RL Submitted (OCT-2010) to the PDB data bank. CC -!- FUNCTION: Has both helicase and E3 ubiquitin ligase activities. CC Possesses intrinsic ATP-dependent nucleosome-remodeling activity; This CC activity may be required for transcriptional activation or repression CC of specific target promoters (By similarity). These may include the CC SERPINE1 and HIV-1 promoters and the SV40 enhancer, to which this CC protein can bind directly. Plays a role in error-free postreplication CC repair (PRR) of damaged DNA and maintains genomic stability through CC acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of CC chromatin-bound PCNA. {ECO:0000250, ECO:0000269|PubMed:10391891, CC ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18719106, CC ECO:0000269|PubMed:7876228, ECO:0000269|PubMed:8672239, CC ECO:0000269|PubMed:9126292}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with SP1 and SP3 independently of DNA; the CC interaction with these transcriptional factors may be required for CC basal transcription of target genes. Interacts with EGR1; the CC interaction requires prior binding to DNA and represses c-Rel via a DNA CC looping mechanism (By similarity). Interacts with GATA4 (By CC similarity). Interacts with PCNA; the interaction promotes CC polyubiquitination of PCNA through association with the UBE2B-RAD18 and CC UBE2V2-UBE2N ubiquitin ligase complexes. Interacts with RAD18, SHPRH, CC UBE2V2 and UBE2N. {ECO:0000250, ECO:0000269|PubMed:10391891, CC ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18719106}. CC -!- INTERACTION: CC Q14527; P12004: PCNA; NbExp=2; IntAct=EBI-1045161, EBI-358311; CC Q14527; Q9NS91: RAD18; NbExp=3; IntAct=EBI-1045161, EBI-2339393; CC Q14527; P60903: S100A10; NbExp=2; IntAct=EBI-1045161, EBI-717048; CC Q14527; P61088: UBE2N; NbExp=4; IntAct=EBI-1045161, EBI-1052908; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000269|PubMed:8672239}. Nucleus, nucleolus {ECO:0000250}. CC Nucleus, nucleoplasm {ECO:0000250}. Note=Nuclear localization is CC stimulated by progesterone. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=Q14527-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14527-2; Sequence=VSP_018873; CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, CC pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:8672239, CC ECO:0000269|PubMed:9126292}. CC -!- MISCELLANEOUS: Subject to frequent epigenetic inactivation by promoter CC methylation in colon cancer. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily. CC {ECO:0000305}. CC -!- CAUTION: In contrast with other SMARC proteins, there is currently no CC evidence that it associates with actin or actin-related proteins. It CC may rather act as a sequence-specific DNA binding ATPase, whose precise CC function remains to be fully characterized. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42332/HLTF"; 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; L34673; AAA67436.1; -; mRNA. DR EMBL; Z46606; CAA86571.1; -; mRNA. DR EMBL; Z46606; CAA86572.1; -; mRNA. DR EMBL; AJ418064; CAD10805.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78889.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78892.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78893.1; -; Genomic_DNA. DR EMBL; BC044659; AAH44659.1; -; mRNA. DR EMBL; S64671; AAB27691.1; -; mRNA. DR CCDS; CCDS33875.1; -. [Q14527-1] DR PIR; S49618; S49618. DR RefSeq; XP_016862568.1; XM_017007079.1. DR PDB; 2MZN; NMR; -; A=51-171. DR PDB; 4HRE; X-ray; 2.79 A; G/H/K/L=26-39. DR PDB; 4HRH; X-ray; 3.00 A; C/D=26-39. DR PDB; 4S0N; X-ray; 1.50 A; A/B/C/D=55-180. DR PDB; 4XZF; X-ray; 1.38 A; A=58-174. DR PDB; 4XZG; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I=57-174. DR PDB; 5BNH; X-ray; 1.70 A; A/D=55-175. DR PDB; 5K5F; NMR; -; A=51-171. DR PDB; 6KCS; X-ray; 2.10 A; A=58-174. DR PDBsum; 2MZN; -. DR PDBsum; 4HRE; -. DR PDBsum; 4HRH; -. DR PDBsum; 4S0N; -. DR PDBsum; 4XZF; -. DR PDBsum; 4XZG; -. DR PDBsum; 5BNH; -. DR PDBsum; 5K5F; -. DR PDBsum; 6KCS; -. DR AlphaFoldDB; Q14527; -. DR BMRB; Q14527; -. DR SMR; Q14527; -. DR BioGRID; 112480; 153. DR ComplexPortal; CPX-856; SMARCA3 - Annexin A2 - S100-A10 complex. DR DIP; DIP-29828N; -. DR IntAct; Q14527; 49. DR MINT; Q14527; -. DR STRING; 9606.ENSP00000308944; -. DR GlyGen; Q14527; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q14527; -. DR PhosphoSitePlus; Q14527; -. DR BioMuta; HLTF; -. DR DMDM; 60390864; -. DR EPD; Q14527; -. DR jPOST; Q14527; -. DR MassIVE; Q14527; -. DR MaxQB; Q14527; -. DR PaxDb; Q14527; -. DR PeptideAtlas; Q14527; -. DR ProteomicsDB; 60030; -. [Q14527-1] DR ProteomicsDB; 60031; -. [Q14527-2] DR Antibodypedia; 18197; 355 antibodies from 33 providers. DR DNASU; 6596; -. DR Ensembl; ENST00000310053.10; ENSP00000308944.5; ENSG00000071794.16. [Q14527-1] DR Ensembl; ENST00000392912.6; ENSP00000376644.2; ENSG00000071794.16. [Q14527-1] DR Ensembl; ENST00000494055.5; ENSP00000420429.1; ENSG00000071794.16. [Q14527-1] DR GeneID; 6596; -. DR KEGG; hsa:6596; -. DR MANE-Select; ENST00000310053.10; ENSP00000308944.5; NM_003071.4; NP_003062.2. DR UCSC; uc003ewq.2; human. [Q14527-1] DR AGR; HGNC:11099; -. DR CTD; 6596; -. DR DisGeNET; 6596; -. DR GeneCards; HLTF; -. DR HGNC; HGNC:11099; HLTF. DR HPA; ENSG00000071794; Low tissue specificity. DR MIM; 603257; gene. DR neXtProt; NX_Q14527; -. DR OpenTargets; ENSG00000071794; -. DR PharmGKB; PA35949; -. DR VEuPathDB; HostDB:ENSG00000071794; -. DR eggNOG; KOG1001; Eukaryota. DR GeneTree; ENSGT00910000144305; -. DR InParanoid; Q14527; -. DR OMA; ETTVWRL; -. DR OrthoDB; 200191at2759; -. DR PhylomeDB; Q14527; -. DR TreeFam; TF332703; -. DR PathwayCommons; Q14527; -. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR SignaLink; Q14527; -. DR SIGNOR; Q14527; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 6596; 12 hits in 1217 CRISPR screens. DR ChiTaRS; HLTF; human. DR GeneWiki; HLTF; -. DR GenomeRNAi; 6596; -. DR Pharos; Q14527; Tbio. DR PRO; PR:Q14527; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q14527; Protein. DR Bgee; ENSG00000071794; Expressed in pons and 221 other tissues. DR ExpressionAtlas; Q14527; baseline and differential. DR Genevisible; Q14527; HS. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; EXP:ComplexPortal. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central. DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; EXP:Reactome. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:ComplexPortal. DR GO; GO:0016567; P:protein ubiquitination; TAS:Reactome. DR GO; GO:0050767; P:regulation of neurogenesis; ISO:ComplexPortal. DR CDD; cd18071; DEXHc_HLTF1_SMARC3; 1. DR CDD; cd16509; RING-HC_HLTF; 1. DR CDD; cd18793; SF2_C_SNF; 1. DR Gene3D; 3.30.70.2330; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014905; HIRAN. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR038718; SNF2-like_sf. DR InterPro; IPR000330; SNF2_N. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR45626:SF22; HELICASE-LIKE TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF08797; HIRAN; 1. DR Pfam; PF00176; SNF2-rel_dom; 1. DR Pfam; PF13923; zf-C3HC4_2; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00910; HIRAN; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative initiation; ATP-binding; KW Chromatin regulator; Cytoplasm; DNA-binding; Helicase; Hydrolase; KW Isopeptide bond; Metal-binding; Methylation; Multifunctional enzyme; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT CHAIN 1..1009 FT /note="Helicase-like transcription factor" FT /id="PRO_0000030722" FT DOMAIN 435..606 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 837..996 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT DNA_BIND 38..287 FT ZN_FING 760..801 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 336..365 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 925..1009 FT /note="Interaction with SP1 and SP3" FT /evidence="ECO:0000269|PubMed:10391891" FT MOTIF 557..560 FT /note="DEGH box" FT BINDING 294..301 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 27 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 195 FT /note="Phosphotyrosine; by JAK2" FT /evidence="ECO:0000269|PubMed:21457752" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 400 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 736 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 112 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 211 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..122 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8672239" FT /id="VSP_018873" FT VARIANT 311 FT /note="N -> S (in dbSNP:rs2305868)" FT /id="VAR_052121" FT VARIANT 362 FT /note="E -> Q (in dbSNP:rs2228257)" FT /id="VAR_052122" FT VARIANT 819 FT /note="R -> H (in dbSNP:rs2229361)" FT /id="VAR_029265" FT CONFLICT 35 FT /note="P -> L (in Ref. 2; CAA86571)" FT /evidence="ECO:0000305" FT CONFLICT 211..213 FT /note="KTE -> PEF (in Ref. 6; AAB27691)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="D -> G (in Ref. 2; CAA86571/CAA86572 and 3; FT CAD10805)" FT /evidence="ECO:0000305" FT CONFLICT 382 FT /note="S -> T (in Ref. 1; AAA67436)" FT /evidence="ECO:0000305" FT CONFLICT 429 FT /note="Missing (in Ref. 5; AAH44659)" FT /evidence="ECO:0000305" FT CONFLICT 913 FT /note="K -> R (in Ref. 2; CAA86571/CAA86572 and 3; FT CAD10805)" FT /evidence="ECO:0000305" FT HELIX 51..54 FT /evidence="ECO:0007829|PDB:2MZN" FT STRAND 58..68 FT /evidence="ECO:0007829|PDB:4XZF" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:4XZF" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:4XZF" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:4XZF" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:4XZF" FT HELIX 113..124 FT /evidence="ECO:0007829|PDB:4XZF" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:4XZF" FT STRAND 141..152 FT /evidence="ECO:0007829|PDB:4XZF" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:4XZF" FT HELIX 157..166 FT /evidence="ECO:0007829|PDB:4XZF" SQ SEQUENCE 1009 AA; 113929 MW; 0AB96F6C8484FD15 CRC64; MSWMFKRDPV WKYLQTVQYG VHGNFPRLSY PTFFPRFEFQ DVIPPDDFLT SDEEVDSVLF GSLRGHVVGL RYYTGVVNNN EMVALQRDPN NPYDKNAIKV NNVNGNQVGH LKKELAGALA YIMDNKLAQI EGVVPFGANN AFTMPLHMTF WGKEENRKAV SDQLKKHGFK LGPAPKTLGF NLESGWGSGR AGPSYSMPVH AAVQMTTEQL KTEFDKLFED LKEDDKTHEM EPAEAIETPL LPHQKQALAW MVSRENSKEL PPFWEQRNDL YYNTITNFSE KDRPENVHGG ILADDMGLGK TLTAIAVILT NFHDGRPLPI ERVKKNLLKK EYNVNDDSMK LGGNNTSEKA DGLSKDASRC SEQPSISDIK EKSKFRMSEL SSSRPKRRKT AVQYIESSDS EEIETSELPQ KMKGKLKNVQ SETKGRAKAG SSKVIEDVAF ACALTSSVPT TKKKMLKKGA CAVEGSKKTD VEERPRTTLI ICPLSVLSNW IDQFGQHIKS DVHLNFYVYY GPDRIREPAL LSKQDIVLTT YNILTHDYGT KGDSPLHSIR WLRVILDEGH AIRNPNAQQT KAVLDLESER RWVLTGTPIQ NSLKDLWSLL SFLKLKPFID REWWHRTIQR PVTMGDEGGL RRLQSLIKNI TLRRTKTSKI KGKPVLELPE RKVFIQHITL SDEERKIYQS VKNEGRATIG RYFNEGTVLA HYADVLGLLL RLRQICCHTY LLTNAVSSNG PSGNDTPEEL RKKLIRKMKL ILSSGSDEEC AICLDSLTVP VITHCAHVFC KPCICQVIQN EQPHAKCPLC RNDIHEDNLL ECPPEELARD SEKKSDMEWT SSSKINALMH ALTDLRKKNP NIKSLVVSQF TTFLSLIEIP LKASGFVFTR LDGSMAQKKR VESIQCFQNT EAGSPTIMLL SLKAGGVGLN LSAASRVFLM DPAWNPAAED QCFDRCHRLG QKQEVIITKF IVKDSVEENM LKIQNKKREL AAGAFGTKKP NADEMKQAKI NEIRTLIDL //