GenomeNet

Database: UniProt
Entry: Q6PCN7
LinkDB: Q6PCN7
Original site: Q6PCN7 
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   11-DEC-2019, entry version 154.
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};
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   BioGrid; 203335; 3.
DR   ComplexPortal; CPX-899; SMARCA3 - Annexin A2 - S100-A10 complex.
DR   IntAct; Q6PCN7; 2.
DR   STRING; 10090.ENSMUSP00000002502; -.
DR   iPTMnet; Q6PCN7; -.
DR   PhosphoSitePlus; Q6PCN7; -.
DR   EPD; Q6PCN7; -.
DR   MaxQB; Q6PCN7; -.
DR   PaxDb; Q6PCN7; -.
DR   PeptideAtlas; Q6PCN7; -.
DR   PRIDE; Q6PCN7; -.
DR   Ensembl; ENSMUST00000002502; ENSMUSP00000002502; ENSMUSG00000002428.
DR   GeneID; 20585; -.
DR   KEGG; mmu:20585; -.
DR   UCSC; uc008osk.1; mouse.
DR   CTD; 6596; -.
DR   MGI; MGI:1196437; Hltf.
DR   eggNOG; ENOG410INU2; Eukaryota.
DR   eggNOG; ENOG410XQ1S; LUCA.
DR   GeneTree; ENSGT00910000144305; -.
DR   HOGENOM; HOG000172619; -.
DR   InParanoid; Q6PCN7; -.
DR   KO; K15711; -.
DR   OMA; RQVCNHW; -.
DR   OrthoDB; 132523at2759; -.
DR   PhylomeDB; Q6PCN7; -.
DR   TreeFam; TF332703; -.
DR   Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   UniPathway; UPA00143; -.
DR   ChiTaRS; Hltf; mouse.
DR   PRO; PR:Q6PCN7; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q6PCN7; protein.
DR   Bgee; ENSMUSG00000002428; Expressed in 288 organ(s), highest expression level in cochlea.
DR   ExpressionAtlas; Q6PCN7; baseline and differential.
DR   Genevisible; Q6PCN7; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:MGI.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 2.
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_N; 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   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   NP_BIND         294..301
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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          919..1003
FT                   /note="Interaction with SP1 and SP3"
FT                   /evidence="ECO:0000250"
FT   MOTIF           551..554
FT                   /note="DEGH box"
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
//
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