HLTF_HUMAN
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 03-AUG-2022, entry version 201.
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="http://atlasgeneticsoncology.org/Genes/HLTFID42332ch3q24.html";
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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; NP_001305863.1; NM_001318934.1.
DR RefSeq; NP_001305864.1; NM_001318935.1. [Q14527-1]
DR RefSeq; NP_003062.2; NM_003071.3. [Q14527-1]
DR RefSeq; NP_620636.1; NM_139048.2. [Q14527-1]
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; 136.
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 PRIDE; Q14527; -.
DR ProteomicsDB; 60030; -. [Q14527-1]
DR ProteomicsDB; 60031; -. [Q14527-2]
DR Antibodypedia; 18197; 318 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 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; VGVMSNW; -.
DR OrthoDB; 132523at2759; -.
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; 11 hits in 1138 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; IC: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; IC: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; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
DR GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 2.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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
