HELZ2_MOUSE
ID HELZ2_MOUSE Reviewed; 2947 AA.
AC E9QAM5; B9A0U1;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Helicase with zinc finger domain 2;
DE EC=3.6.4.-;
DE AltName: Full=PPAR-gamma DNA-binding domain-interacting protein 1;
DE Short=PDIP1;
DE Short=PPAR-gamma DBD-interacting protein 1;
GN Name=Helz2;
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 [MRNA].
RA Yoshino S., Satoh T., Tomaru T., Ishizuka T., Hashimoto K., Monden T.,
RA Yamada M., Mori M.;
RT "Molecular cloning and characterization of the mouse PDIP1.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=16239304; DOI=10.1210/en.2005-0450;
RA Tomaru T., Satoh T., Yoshino S., Ishizuka T., Hashimoto K., Monden T.,
RA Yamada M., Mori M.;
RT "Isolation and characterization of a transcriptional cofactor and its novel
RT isoform that bind the DNA-binding domain of peroxisome proliferator-
RT activated receptor gamma.";
RL Endocrinology 147:377-388(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, and Spleen;
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, INTERACTION WITH PPARG AND THRAP3, AND SUBCELLULAR LOCATION.
RX PubMed=23525231; DOI=10.1210/me.2012-1332;
RA Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S.,
RA Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K.,
RA Okada S., Yamada M., Mori M.;
RT "THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
RT differentiation.";
RL Mol. Endocrinol. 27:769-780(2013).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Helicase that acts as a transcriptional coactivator for a
CC number of nuclear receptors including PPARA, PPARG, THRA, THRB and
CC RXRA. {ECO:0000269|PubMed:23525231}.
CC -!- SUBUNIT: Interacts with PPARA (via DNA-binding domain) and PPARG; the
CC interaction stimulates the transcriptional activity of PPARA and PPARG.
CC Interacts with THRAP3; the interaction is direct and HELZ2 and THRAP3
CC synergistically enhance the transcriptional activity of PPARG. It is
CC probably part of the peroxisome proliferator activated receptor alpha
CC interacting complex (PRIC). {ECO:0000269|PubMed:23525231}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}.
CC -!- DEVELOPMENTAL STAGE: In 3T3-L1 cell line, highly expressed before
CC differentiation with a slight decreased after the induction of
CC adipocyte differentiation. {ECO:0000269|PubMed:16239304}.
CC -!- DOMAIN: Contains 5 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. These motifs are
CC not required for interaction with PPARG (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; AB201714; BAH20441.1; -; mRNA.
DR EMBL; AL845506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38380.1; -.
DR RefSeq; NP_898985.2; NM_183162.2.
DR RefSeq; XP_006500662.1; XM_006500599.3.
DR SMR; E9QAM5; -.
DR BioGRID; 230806; 16.
DR IntAct; E9QAM5; 1.
DR MINT; E9QAM5; -.
DR STRING; 10090.ENSMUSP00000091756; -.
DR iPTMnet; E9QAM5; -.
DR PhosphoSitePlus; E9QAM5; -.
DR SwissPalm; E9QAM5; -.
DR EPD; E9QAM5; -.
DR MaxQB; E9QAM5; -.
DR PaxDb; E9QAM5; -.
DR PRIDE; E9QAM5; -.
DR ProteomicsDB; 269582; -.
DR Antibodypedia; 63897; 47 antibodies from 17 providers.
DR Ensembl; ENSMUST00000108831; ENSMUSP00000104459; ENSMUSG00000027580.
DR GeneID; 229003; -.
DR KEGG; mmu:229003; -.
DR UCSC; uc008oln.1; mouse.
DR CTD; 85441; -.
DR MGI; MGI:2385169; Helz2.
DR VEuPathDB; HostDB:ENSMUSG00000027580; -.
DR eggNOG; KOG1804; Eukaryota.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00940000160694; -.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 229003; 1 hit in 76 CRISPR screens.
DR PRO; PR:E9QAM5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; E9QAM5; protein.
DR Bgee; ENSMUSG00000027580; Expressed in lymph node and 184 other tissues.
DR ExpressionAtlas; E9QAM5; baseline and differential.
DR Genevisible; E9QAM5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR CDD; cd18808; SF1_C_Upf1; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR031191; HELZ2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF428; PTHR10887:SF428; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 2.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; DNA-binding; Helicase; Hydrolase; Metal-binding;
KW Methylation; Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..2947
FT /note="Helicase with zinc finger domain 2"
FT /id="PRO_0000424355"
FT ZN_FING 167..187
FT /note="C2H2-type"
FT ZN_FING 289..311
FT /note="C2H2-type; atypical"
FT REGION 809..1290
FT /note="Interaction with THRAP3"
FT /evidence="ECO:0000250"
FT REGION 1260..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2413..2947
FT /note="Interaction with THRAP3"
FT /evidence="ECO:0000250"
FT MOTIF 913..916
FT /note="DEAA box"
FT MOTIF 1306..1310
FT /note="LXXLL motif 1"
FT MOTIF 1348..1352
FT /note="LXXLL motif 2"
FT MOTIF 1403..1407
FT /note="LXXLL motif 3"
FT MOTIF 2240..2244
FT /note="LXXLL motif 4"
FT MOTIF 2525..2529
FT /note="LXXLL motif 5"
FT BINDING 790..797
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2470..2477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2381
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 348
FT /note="E -> G (in Ref. 1; BAH20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="R -> C (in Ref. 1; BAH20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="F -> S (in Ref. 1; BAH20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="T -> A (in Ref. 1; BAH20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 1301
FT /note="A -> T (in Ref. 1; BAH20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 1316
FT /note="V -> A (in Ref. 1; BAH20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 2337
FT /note="D -> E (in Ref. 1; BAH20441)"
FT /evidence="ECO:0000305"
FT CONFLICT 2639
FT /note="S -> C (in Ref. 1; BAH20441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2947 AA; 331563 MW; 7B82DF8713B34988 CRC64;
MASVGCSLRS ASTSATNGPS LAGLCAKVDL YLGCSRCTQC LNESTYILRE VEHTCPREIL
LARFKQAAES KIWRKVGRRP SFPTPMRYQV CHYYRPGLGC RRHWNRCTFA RSPEEALVWT
FELKNNLPRL KLKEAVQGTR APDRLQTPAD TIRAEFGGHF QLLCAICFTC CPPCLCPVDP
RGHCPKHQIC PTLLIHVIVE GLKRQFVEVR PLPQRRHPLN YCMYVGRGVP CRHGASRCEY
AHSAVEMAVW KAEQLDGLQR GDLLTYPLFG ENKWKASPNP NPPVTKLYCH ACLVTCNSQE
AFENHCSSLE HAQMVAFDQA VPWKHRAPPM GLSKFDLCPR PDLCEHGEVC IKAHSKQELQ
EWVQRAQDME LREQAAWQDG LVPYQARLLA EYQRSSKEVS VMAETIRGVS VTCHPPPVHQ
AQEKIQHQWV FTIHSEDPLL HVALLNQEPG AAFSLVAPSL PPHQLYAQGK HFCVQSSPAQ
YKVGVLVQAV AFGSFEQWVV FDFGRRPVLL QKLKLQLGQT HSQGLNGKPA PSHPQELECW
HTGNRHVVLE VDWTPEQEAL MAKYKLPSLA LEFNQIVPDW GPISRSNYRQ RMHKFLYEEE
AAQQQLVAKL AMKGQVSLKT ALETPALGML FAPPGALYAK VPFHSSLLPD TDQGFLLSRA
VSTALVAPVP APNSTVYQVR LEARASSDHA LWLLLPARCC MALGLQAQDS PILEVQFQID
PMTFRFWHQA VDALLEEHLV VPDLPACTLP HPWPTPPSFR GNHKQKLAVG LIAGRRPEGT
KHIPPLLIYG PFGTGKTYTL AMAALEVVQQ PHTKVLICTH TNSAADIYIR EYFHDYVSSG
HPEATPLRVM YADRPPRQTD PTTLQYCCLT EDRQAFRPPT GPELVHHRLV VTTTSQAREL
QVPAGFFSHI FIDEAAQMLE CEALIPLSYA LSLTRVVLAG DHMQVTPRLF SVPRDKSARH
TLLHRLFLYY QQEAHKIAQQ SRIIFHENYR STAAIINFVS HHFYLAKGNP IQASGKVPRH
PQHYPLMFCH VAGSPEQDMS MTSWLNSAEV TQVVEKVREI YNTWPHCWGP REQRHICAVS
HGAQVSALRQ ELRRRNLGEV SVGSFEILPG REFRVVVLSS VHNRNSLLSP GAPTSEFFTE
PRVLNTVMTR AQSQLVAVGD AVALCSSGAC RNLWRSFIRE CIEHHSAFPE ELSLEQIEQG
VAQRQNWASL TLKARGPETE QKSMAQGPQR LIAEGTMVTV KAETRAEAAA KAQTAAVAAE
DTASGNSASR DAAAEVSTLE GGMSEEDSES DFWPSDWELN ADDAILKELL DESQQVTVTV
REDGLLDTVV CSAPQKAREY TNLPSSVLWK FLRSNSKQFR RCSFLQETFE RALATPLDDM
ASSPIQVRGR LNCGMAFTGD EVLVQILGPA GDDRCVPGSL QGRVMGVLKR RRHELAFVCR
MDEWDPRIMI PINGSVTKIF VAEMKDPQQV PIHRLIQGQV QRVRHETLKP EDRSTRLFWV
RIVLWRERFY YPLGIVLEVL PKAITWEQGL YILDLEHGLK AHTPDPASVS KALQRYRSEL
NTAAGHREDY RHFLTFTVDP QGACNLDDAL SVRDLGPVYE VAVHIADVAS LVPKDGALDV
EARQQGTVFY APNREPVLML PASLCQDALS LLPGQDRLAI SLFLTMEKGG GQIKSLRFAP
SIIRSDRQLS YEEAEELIKR HPGAGLELPA HLDSVEACVV AACYFSWMLR RQRLSAACYY
EPPDEDSVLG FRTAHIMVQE YMIQFNSHVA EFLVSNKHTQ TLTPLRWQPT PSRQQLDSVF
KKYRGLVPLS LHLCHHSNTD YTPNKQLHLL TSLWKQVQLA AGTQDYSQMV DLIAADDMHP
SLAPACLDLR RALGRSVFGR SSQGKQQPAV HHSLQVDWYT WATSPIRRYL DVVLQRLILL
ALGHRGSTYS NRDIDGLCLD FSRQYASAQS YQRRAYSLHL AIQLKSQPQN KLGFVVDVEM
GARCFKVLFP INRETLPDPC PIHYHSLQLA EHPQELVSQT GVRLVWRRRM YSVQASKLPL
PLLGTSLDPH TQTVDAALWM KLLMLLKEQR WPEIAALIQE QDKRFHPREK VKIHQSRCGH
FVEVVYELGS GDTLQVQLGS SLQRGFLAPT LKLWTVVPGF SLCLEHMERP GDCFSSHVHQ
ALQDQYLQVG EYSGAWGPRC ALESLTNAVT ENDSIVLHDV HISWDTSQGQ LQGTFQLEAA
FLQEKCINIH FGCCYLCIRL EGLPLPLDSS LPGPSGLGPF LNIDPNTYTW VAHGLSGDWD
HELAGGDWDQ ENVDDRQEAP KQVYFLIHHM TMEKVPEEVL RPSARFTVEV LSKQLPDLRK
EEAVRQLKTA SPLVISIALG LPIPEIRWPI SGPRRLVSEL RWPIPGPRRP VSEPHRPMSG
PCGPISEPCR SIPEPCRGNW PRQHSFHKAS TSRFLERQNY NIPAGHHKLN QSQDRAVRSA
LQKQFTVIQG PPGTGKTVVG FHIVYWFHRS NQEQMPTDSS PSGEEQLGGP CVLYCGPSNK
SVDVLGGLLL RRKTEMKPLR VYGEQAEATE FPLPGVSNRS LFGKTSQEGR PNQSLRSITL
HHRIRQAPNP YAAEIRKFDA QLREGKIFSK EDLRVYRRVL GKARKHELER HSVILCTCSC
AASKSLKILN VRQILIDEAG MATEPETLIP LVCFSKTVEK VVLLGDHKQL RPVVKSEQLQ
SLGMDRSLFE RYHRDAIMLD TQYRMHKDIC SFPSVEFYGG KLKTWSDLRR LPSILGHTGK
PSCSVIFGSV QGHEQKLLVS TEDGNENSRA NPEEVTQVVR IIKQLTLDRT VDPKDIAVLT
PYNAQAAAIS RGLMQRGVTG VTVTSITKSQ GSEWRYVIVS TVRTCPRSDV DQRPTKSWLK
KFLGFVVDPH QVNVAITRAQ EALCIIGDHL LLRCCPLWHR LLDFCEAQHS LVSAEKVRVQ
RKSALSS
