ID HLTF_MOUSE Reviewed; 1003 AA.
AC Q6PCN7; O35596; O35597; Q80VT6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=Helicase-like transcription factor;
DE EC=2.3.2.27;
DE EC=3.6.4.-;
DE AltName: Full=P113;
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;
DE AltName: Full=TNF-response element-binding protein;
GN Name=Hltf; Synonyms=Smarca3, Snf2l3, Zbu1;
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC TISSUE=Liver;
RX PubMed=9427542; DOI=10.1016/s0378-1119(97)00446-0;
RA Zhang Q., Ekhterae D., Kim K.-H.;
RT "Molecular cloning and characterization of P113, a mouse SNF2/SWI2-related
RT transcription factor.";
RL Gene 202:31-37(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
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, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [4]
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).
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, to which this protein can bind directly. Plays a role in
CC error-free postreplication repair (PRR) of damaged DNA and maintains
CC genomic stability through acting as a ubiquitin ligase for 'Lys-63'-
CC linked polyubiquitination of chromatin-bound PCNA (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:9126292, ECO:0000269|PubMed:9427542}.
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. Interacts with GATA4. Interacts with PCNA; the
CC interaction promotes polyubiquitination of PCNA through association
CC with the UBE2B-RAD18 and UBE2V2-UBE2N ubiquitin ligase complexes.
CC Interacts with RAD18, SHPRH, UBE2V2 and UBE2N (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:9427542}. Nucleus, nucleolus {ECO:0000250}.
CC Nucleus, nucleoplasm {ECO:0000250}. Note=Nuclear localization is
CC stimulated by progesterone. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:9126292}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the heart from 11.5 dpc. Gradually
CC increases in skeletal muscle to 18.5 dpc. {ECO:0000269|PubMed:9126292}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63915.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF010138; AAB64175.1; -; Genomic_DNA.
DR EMBL; AF010600; AAB63915.1; ALT_SEQ; mRNA.
DR EMBL; BC039796; AAH39796.1; -; mRNA.
DR EMBL; BC057116; AAH57116.1; -; mRNA.
DR EMBL; BC059240; AAH59240.1; -; mRNA.
DR CCDS; CCDS17261.1; -.
DR RefSeq; NP_033236.2; NM_009210.3.
DR RefSeq; XP_006535491.1; XM_006535428.3.
DR AlphaFoldDB; Q6PCN7; -.
DR SMR; Q6PCN7; -.
DR BioGRID; 203335; 7.
DR ComplexPortal; CPX-899; SMARCA3 - Annexin A2 - S100-A10 complex.
DR IntAct; Q6PCN7; 3.
DR STRING; 10090.ENSMUSP00000002502; -.
DR iPTMnet; Q6PCN7; -.
DR PhosphoSitePlus; Q6PCN7; -.
DR EPD; Q6PCN7; -.
DR MaxQB; Q6PCN7; -.
DR PaxDb; 10090-ENSMUSP00000002502; -.
DR PeptideAtlas; Q6PCN7; -.
DR ProteomicsDB; 273363; -.
DR Pumba; Q6PCN7; -.
DR Antibodypedia; 18197; 362 antibodies from 33 providers.
DR DNASU; 20585; -.
DR Ensembl; ENSMUST00000002502.12; ENSMUSP00000002502.6; ENSMUSG00000002428.13.
DR GeneID; 20585; -.
DR KEGG; mmu:20585; -.
DR UCSC; uc008osk.1; mouse.
DR AGR; MGI:1196437; -.
DR MGI; MGI:1196437; Hltf.
DR VEuPathDB; HostDB:ENSMUSG00000002428; -.
DR eggNOG; KOG1001; Eukaryota.
DR GeneTree; ENSGT00910000144305; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; Q6PCN7; -.
DR OMA; ETTVWRL; -.
DR OrthoDB; 200191at2759; -.
DR PhylomeDB; Q6PCN7; -.
DR TreeFam; TF332703; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 20585; 3 hits in 120 CRISPR screens.
DR ChiTaRS; Hltf; mouse.
DR PRO; PR:Q6PCN7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6PCN7; Protein.
DR Bgee; ENSMUSG00000002428; Expressed in saccule of membranous labyrinth and 262 other cell types or tissues.
DR ExpressionAtlas; Q6PCN7; baseline and differential.
DR Genevisible; Q6PCN7; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:MGI.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO: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; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0050767; P:regulation of neurogenesis; IDA: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; IPR049730; SNF2/RAD54-like_C.
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:SF17; 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 Activator; ATP-binding; Chromatin regulator; Cytoplasm; DNA-binding;
KW Helicase; Hydrolase; Isopeptide bond; Metal-binding; Methylation;
KW Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1003
FT /note="Helicase-like transcription factor"
FT /id="PRO_0000056185"
FT DOMAIN 433..600
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 831..990
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 754..795
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 38..287
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 317..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..1003
FT /note="Interaction with SP1 and SP3"
FT /evidence="ECO:0000250"
FT MOTIF 551..554
FT /note="DEGH box"
FT COMPBIAS 317..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q14527"
FT MOD_RES 195
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000269|PubMed:21457752"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14527"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14527"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14527"
FT MOD_RES 730
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14527"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14527"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14527"
FT CONFLICT 150
FT /note="F -> Y (in Ref. 1; AAB64175/AAB63915)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> R (in Ref. 1; AAB64175/AAB63915)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="S -> N (in Ref. 1; AAB64175/AAB63915)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="P -> S (in Ref. 1; AAB64175/AAB63915)"
FT /evidence="ECO:0000305"
FT CONFLICT 902..905
FT /note="MLLS -> STV (in Ref. 1; AAB64175)"
FT /evidence="ECO:0000305"
FT CONFLICT 918
FT /note="A -> R (in Ref. 1; AAB64175)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="G -> A (in Ref. 1; AAB64175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 113317 MW; 91F08509ACEA5513 CRC64;
MSYTFTRGPV WKYSQSVQYG SHENIPRLSY STFLPHFEFQ DIIPPDDFLT SDEEQDLVLF
GTMRGQVVGL RYYTGVVNNN EMVALQREPN NPYDKNAIKV NNVNGNQVGH IKREIAAAVA
YIMDNKLAQV EGVVPFGASN TFTMPLYMTF WGKEENRNVV LEQLKKHGFK LGPTPKTLGS
SLENAWGSGR AGPSYSRPAH VAVQMTTDQL KTEFDKLFED LKEDDRTVEM EPAEAIETPL
LPHQKQALAW MIARENSKEL PPFWEQRNDL YYNTITNFSV KERPENVHGG ILADDMGLGK
TLTAIAVILT NFDDGRPLLS KRGKKNHPGK EYKDETIKRR GSNMDKKEDG HSESSTCGEE
PSISGTPEKS SCTLSQLSSV CPKRRKISVQ YIESSDSEEI ETSELPQKMK GKLKNVQLNT
KSRVKGSSKV KEDSKFALTF FASATQRKML KKGMSMMECS EACDTGERTR ATLIICPLSV
LSNWIDQFGQ HVKSEVHLNF YVYYGPDRIR DSAWLSKQDI ILTTYNILTH DYGTKDDSPL
HSIKWLRVIL DEGHAIRNPN AQQTKAVLEL EAERRWVLTG TPIQNSLKDL WSLLSFLKLK
PFIDREWWYR IIQRPVTTGD EGGLRRLQSL IKNITLRRTK TSKIKGKPVL ELPERKVFIQ
HITLSEEERK IYQSVKNEGK AAIGRYFTEG TVLAHYADVL GLLLRLRQIC CHTHLLTNGM
SSSGPSRSDT PEELRKMLIE KMKIILSSGS DEECAICLDS LTFPVITHCA HVFCKPCICQ
VIHSEQPHAK CPLCRNEIHG DNLLECPPEE LACDSDKESS MEWKSSSKIN ALMHALIELR
TKDPNIKSLV VSQFTTFLSL IETPLKASGF VFTRLDGSMA QKKRVESIQR FQNTEAGSPT
IMLLSLKAGG VGLNLCAASR VFLMDPAWNP AAEDQCFDRC HRLGQKQEVI ITKFIVKDSV
EENMLKIQNT KRDLAAGAFG TKKTDANDMK QAKINEIRTL IDL
//
