Full text data of HELLS
HELLS
(PASG, SMARCA6)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Lymphoid-specific helicase; 3.6.4.- (Proliferation-associated SNF2-like protein; SWI/SNF2-related matrix-associated actin-dependent regulator of chromatin subfamily A member 6)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Lymphoid-specific helicase; 3.6.4.- (Proliferation-associated SNF2-like protein; SWI/SNF2-related matrix-associated actin-dependent regulator of chromatin subfamily A member 6)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00010590
IPI00010590 Proliferation-associated factor Proliferation-associated factor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a not mentioned n/a expected molecular weight found in band between 17-25 kDa
IPI00010590 Proliferation-associated factor Proliferation-associated factor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a not mentioned n/a expected molecular weight found in band between 17-25 kDa
UniProt
Q9NRZ9
ID HELLS_HUMAN Reviewed; 838 AA.
AC Q9NRZ9; B2RB41; Q3LID1; Q6I7N7; Q76H76; Q76H77; Q76H78; Q76H79;
read moreAC Q76H80; Q76H81; Q7Z397; Q7Z5X2; Q8N6P4; Q9H4P5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Lymphoid-specific helicase;
DE EC=3.6.4.-;
DE AltName: Full=Proliferation-associated SNF2-like protein;
DE AltName: Full=SWI/SNF2-related matrix-associated actin-dependent regulator of chromatin subfamily A member 6;
GN Name=HELLS; Synonyms=PASG, SMARCA6; ORFNames=Nbla10143;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=10910076;
RA Lee D.W., Zhang K., Ning Z.-Q., Raabe E.H., Tintner S., Wieland R.,
RA Wilkins B.J., Kim J.M., Blough R.I., Arceci R.J.;
RT "Proliferation-associated SNF2-like gene (PASG): a SNF2 family member
RT altered in leukemia.";
RL Cancer Res. 60:3612-3622(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6; 7; 8 AND 9).
RX PubMed=15305370; DOI=10.1002/ijc.20407;
RA Yano M., Ouchida M., Shigematsu H., Tanaka N., Ichimura K.,
RA Kobayashi K., Inaki Y., Toyooka S., Tsukuda K., Shimizu N.,
RA Shimizu K.;
RT "Tumor-specific exon creation of the HELLS/SMARCA6 gene in non-small
RT cell lung cancer.";
RL Int. J. Cancer 112:8-13(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 415-838 (ISOFORMS 1/2/3).
RC TISSUE=Bone marrow, Prostate, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 464-838 (ISOFORMS
RP 1/2/3/5/6).
RC TISSUE=Brain;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 467-838 (ISOFORMS
RP 1/2/3/5/6).
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of
RT the genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP VARIANT ARG-616.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT gene PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Plays an essential role in normal development and
CC survival. Involved in regulation of the expansion or survival of
CC lymphoid cells. Required for de novo or maintenance DNA
CC methylation. May control silencing of the imprinted CDKN1C gene
CC through DNA methylation. May play a role in formation and
CC organization of heterochromatin, implying a functional role in the
CC regulation of transcription and mitosis (By similarity).
CC -!- INTERACTION:
CC O00716:E2F3; NbExp=2; IntAct=EBI-1056215, EBI-765551;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Closely
CC associated with pericentric heterochromatin (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q9NRZ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRZ9-2; Sequence=VSP_052224;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9NRZ9-3; Sequence=VSP_052228;
CC Name=4;
CC IsoId=Q9NRZ9-4; Sequence=VSP_052234;
CC Name=5;
CC IsoId=Q9NRZ9-5; Sequence=VSP_052231;
CC Name=6;
CC IsoId=Q9NRZ9-6; Sequence=VSP_052227;
CC Name=7;
CC IsoId=Q9NRZ9-7; Sequence=VSP_052232, VSP_052233;
CC Name=8;
CC IsoId=Q9NRZ9-8; Sequence=VSP_052229, VSP_052230;
CC Name=9;
CC IsoId=Q9NRZ9-9; Sequence=VSP_052225, VSP_052226;
CC -!- TISSUE SPECIFICITY: Highly expressed in proliferative tissues such
CC as adult thymus and testis, and expressed at lower levels in
CC uterus, small intestine, colon, and peripheral blood mononuclear
CC cells. Also expressed in neoplastic cell lines including those
CC derived from myeloid and lymphoid leukemias.
CC -!- INDUCTION: By concanavalin-A in peripheral blood leukocytes.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01987.1; Type=Erroneous initiation;
CC Sequence=AAH29381.1; Type=Erroneous initiation;
CC Sequence=AAH30963.1; Type=Erroneous initiation;
CC Sequence=AAH31004.1; Type=Erroneous initiation;
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DR EMBL; AF155827; AAF82262.1; -; mRNA.
DR EMBL; AB102717; BAD10845.1; -; mRNA.
DR EMBL; AB102718; BAD10846.1; -; mRNA.
DR EMBL; AB102719; BAD10847.1; -; mRNA.
DR EMBL; AB102720; BAD10848.1; -; mRNA.
DR EMBL; AB102721; BAD10849.1; -; mRNA.
DR EMBL; AB102722; BAD10850.1; -; mRNA.
DR EMBL; AK314485; BAG37088.1; -; mRNA.
DR EMBL; AB113249; BAD24805.1; -; mRNA.
DR EMBL; BX538033; CAD97978.1; -; mRNA.
DR EMBL; AL138759; CAD13191.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50035.1; -; Genomic_DNA.
DR EMBL; BC015477; AAH15477.1; -; mRNA.
DR EMBL; BC029381; AAH29381.1; ALT_INIT; mRNA.
DR EMBL; BC030963; AAH30963.1; ALT_INIT; mRNA.
DR EMBL; BC031004; AAH31004.1; ALT_INIT; mRNA.
DR EMBL; AY007108; AAG01987.1; ALT_INIT; mRNA.
DR EMBL; AB074174; BAE45737.1; -; mRNA.
DR RefSeq; NP_060533.2; NM_018063.3.
DR RefSeq; XP_005269782.1; XM_005269725.1.
DR RefSeq; XP_005269783.1; XM_005269726.1.
DR RefSeq; XP_005269784.1; XM_005269727.1.
DR RefSeq; XP_005269785.1; XM_005269728.1.
DR UniGene; Hs.655830; -.
DR ProteinModelPortal; Q9NRZ9; -.
DR SMR; Q9NRZ9; 214-486, 510-743.
DR IntAct; Q9NRZ9; 5.
DR MINT; MINT-2819086; -.
DR PhosphoSite; Q9NRZ9; -.
DR DMDM; 74761670; -.
DR PaxDb; Q9NRZ9; -.
DR PRIDE; Q9NRZ9; -.
DR DNASU; 3070; -.
DR Ensembl; ENST00000348459; ENSP00000239027; ENSG00000119969.
DR Ensembl; ENST00000394036; ENSP00000377601; ENSG00000119969.
DR Ensembl; ENST00000394044; ENSP00000377608; ENSG00000119969.
DR Ensembl; ENST00000394045; ENSP00000377609; ENSG00000119969.
DR GeneID; 3070; -.
DR KEGG; hsa:3070; -.
DR UCSC; uc001kjs.3; human.
DR CTD; 3070; -.
DR GeneCards; GC10P096305; -.
DR H-InvDB; HIX0017337; -.
DR HGNC; HGNC:4861; HELLS.
DR HPA; CAB004491; -.
DR MIM; 603946; gene.
DR neXtProt; NX_Q9NRZ9; -.
DR PharmGKB; PA35054; -.
DR eggNOG; COG0553; -.
DR HOVERGEN; HBG060049; -.
DR OrthoDB; EOG7TXKG5; -.
DR PhylomeDB; Q9NRZ9; -.
DR ChiTaRS; HELLS; human.
DR GeneWiki; HELLS; -.
DR GenomeRNAi; 3070; -.
DR NextBio; 12147; -.
DR PRO; PR:Q9NRZ9; -.
DR ArrayExpress; Q9NRZ9; -.
DR Bgee; Q9NRZ9; -.
DR Genevestigator; Q9NRZ9; -.
DR GO; GO:0005721; C:centromeric heterochromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031508; P:centromeric heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0046651; P:lymphocyte proliferation; ISS:UniProtKB.
DR GO; GO:0010216; P:maintenance of DNA methylation; ISS:UniProtKB.
DR GO; GO:0006346; P:methylation-dependent chromatin silencing; ISS:UniProtKB.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2_N; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Complete proteome; Developmental protein; Helicase;
KW Hydrolase; Mitosis; Nucleotide-binding; Nucleus; Polymorphism;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 838 Lymphoid-specific helicase.
FT /FTId=PRO_0000260051.
FT DOMAIN 235 403 Helicase ATP-binding.
FT DOMAIN 603 767 Helicase C-terminal.
FT NP_BIND 248 255 ATP (By similarity).
FT COILED 30 115 Potential.
FT MOTIF 354 357 DEAH box.
FT VAR_SEQ 1 16 Missing (in isoform 2).
FT /FTId=VSP_052224.
FT VAR_SEQ 124 129 VMRKKR -> GNFVCG (in isoform 9).
FT /FTId=VSP_052225.
FT VAR_SEQ 130 838 Missing (in isoform 9).
FT /FTId=VSP_052226.
FT VAR_SEQ 313 442 Missing (in isoform 6).
FT /FTId=VSP_052227.
FT VAR_SEQ 313 344 Missing (in isoform 3).
FT /FTId=VSP_052228.
FT VAR_SEQ 313 315 VRN -> IYL (in isoform 8).
FT /FTId=VSP_052229.
FT VAR_SEQ 316 838 Missing (in isoform 8).
FT /FTId=VSP_052230.
FT VAR_SEQ 345 442 Missing (in isoform 5).
FT /FTId=VSP_052231.
FT VAR_SEQ 345 345 H -> L (in isoform 7).
FT /FTId=VSP_052232.
FT VAR_SEQ 346 838 Missing (in isoform 7).
FT /FTId=VSP_052233.
FT VAR_SEQ 783 838 Missing (in isoform 4).
FT /FTId=VSP_052234.
FT VARIANT 616 616 H -> R (found in a renal cell carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_064720.
FT CONFLICT 136 136 Y -> F (in Ref. 4; CAD97978).
FT CONFLICT 646 646 D -> N (in Ref. 4; CAD97978).
FT CONFLICT 696 696 W -> C (in Ref. 7; AAH29381).
FT CONFLICT 702 702 L -> P (in Ref. 9; BAE45737).
SQ SEQUENCE 838 AA; 97074 MW; FE8C644C23F2526E CRC64;
MPAERPAGSG GSEAPAMVEQ LDTAVITPAM LEEEEQLEAA GLERERKMLE KARMSWDRES
TEIRYRRLQH LLEKSNIYSK FLLTKMEQQQ LEEQKKKEKL ERKKESLKVK KGKNSIDASE
EKPVMRKKRG REDESYNISE VMSKEEILSV AKKNKKENED ENSSSTNLCV EDLQKNKDSN
SIIKDRLSET VRQNTKFFFD PVRKCNGQPV PFQQPKHFTG GVMRWYQVEG MEWLRMLWEN
GINGILADEM GLGKTVQCIA TIALMIQRGV PGPFLVCGPL STLPNWMAEF KRFTPDIPTM
LYHGTQEERQ KLVRNIYKRK GTLQIHPVVI TSFEIAMRDR NALQHCYWKY LIVDEGHRIK
NMKCRLIREL KRFNADNKLL LTGTPLQNNL SELWSLLNFL LPDVFDDLKS FESWFDITSL
SETAEDIIAK EREQNVLHML HQILTPFLLR RLKSDVALEV PPKREVVVYA PLSKKQEIFY
TAIVNRTIAN MFGSSEKETI ELSPTGRPKR RTRKSINYSK IDDFPNELEK LISQIQPEVD
RERAVVEVNI PVESEVNLKL QNIMMLLRKC CNHPYLIEYP IDPVTQEFKI DEELVTNSGK
FLILDRMLPE LKKRGHKVLL FSQMTSMLDI LMDYCHLRDF NFSRLDGSMS YSEREKNMHS
FNTDPEVFIF LVSTRAGGLG INLTAADTVI IYDSDWNPQS DLQAQDRCHR IGQTKPVVVY
RLVTANTIDQ KIVERAAAKR KLEKLIIHKN HFKGGQSGLN LSKNFLDPKE LMELLKSRDY
EREIKGSREK VISDKDLELL LDRSDLIDQM NASGPIKEKM GIFKILENSE DSSPECLF
//
ID HELLS_HUMAN Reviewed; 838 AA.
AC Q9NRZ9; B2RB41; Q3LID1; Q6I7N7; Q76H76; Q76H77; Q76H78; Q76H79;
read moreAC Q76H80; Q76H81; Q7Z397; Q7Z5X2; Q8N6P4; Q9H4P5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Lymphoid-specific helicase;
DE EC=3.6.4.-;
DE AltName: Full=Proliferation-associated SNF2-like protein;
DE AltName: Full=SWI/SNF2-related matrix-associated actin-dependent regulator of chromatin subfamily A member 6;
GN Name=HELLS; Synonyms=PASG, SMARCA6; ORFNames=Nbla10143;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=10910076;
RA Lee D.W., Zhang K., Ning Z.-Q., Raabe E.H., Tintner S., Wieland R.,
RA Wilkins B.J., Kim J.M., Blough R.I., Arceci R.J.;
RT "Proliferation-associated SNF2-like gene (PASG): a SNF2 family member
RT altered in leukemia.";
RL Cancer Res. 60:3612-3622(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6; 7; 8 AND 9).
RX PubMed=15305370; DOI=10.1002/ijc.20407;
RA Yano M., Ouchida M., Shigematsu H., Tanaka N., Ichimura K.,
RA Kobayashi K., Inaki Y., Toyooka S., Tsukuda K., Shimizu N.,
RA Shimizu K.;
RT "Tumor-specific exon creation of the HELLS/SMARCA6 gene in non-small
RT cell lung cancer.";
RL Int. J. Cancer 112:8-13(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 415-838 (ISOFORMS 1/2/3).
RC TISSUE=Bone marrow, Prostate, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 464-838 (ISOFORMS
RP 1/2/3/5/6).
RC TISSUE=Brain;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 467-838 (ISOFORMS
RP 1/2/3/5/6).
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of
RT the genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP VARIANT ARG-616.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT gene PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Plays an essential role in normal development and
CC survival. Involved in regulation of the expansion or survival of
CC lymphoid cells. Required for de novo or maintenance DNA
CC methylation. May control silencing of the imprinted CDKN1C gene
CC through DNA methylation. May play a role in formation and
CC organization of heterochromatin, implying a functional role in the
CC regulation of transcription and mitosis (By similarity).
CC -!- INTERACTION:
CC O00716:E2F3; NbExp=2; IntAct=EBI-1056215, EBI-765551;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Closely
CC associated with pericentric heterochromatin (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q9NRZ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRZ9-2; Sequence=VSP_052224;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9NRZ9-3; Sequence=VSP_052228;
CC Name=4;
CC IsoId=Q9NRZ9-4; Sequence=VSP_052234;
CC Name=5;
CC IsoId=Q9NRZ9-5; Sequence=VSP_052231;
CC Name=6;
CC IsoId=Q9NRZ9-6; Sequence=VSP_052227;
CC Name=7;
CC IsoId=Q9NRZ9-7; Sequence=VSP_052232, VSP_052233;
CC Name=8;
CC IsoId=Q9NRZ9-8; Sequence=VSP_052229, VSP_052230;
CC Name=9;
CC IsoId=Q9NRZ9-9; Sequence=VSP_052225, VSP_052226;
CC -!- TISSUE SPECIFICITY: Highly expressed in proliferative tissues such
CC as adult thymus and testis, and expressed at lower levels in
CC uterus, small intestine, colon, and peripheral blood mononuclear
CC cells. Also expressed in neoplastic cell lines including those
CC derived from myeloid and lymphoid leukemias.
CC -!- INDUCTION: By concanavalin-A in peripheral blood leukocytes.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01987.1; Type=Erroneous initiation;
CC Sequence=AAH29381.1; Type=Erroneous initiation;
CC Sequence=AAH30963.1; Type=Erroneous initiation;
CC Sequence=AAH31004.1; Type=Erroneous initiation;
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DR EMBL; AF155827; AAF82262.1; -; mRNA.
DR EMBL; AB102717; BAD10845.1; -; mRNA.
DR EMBL; AB102718; BAD10846.1; -; mRNA.
DR EMBL; AB102719; BAD10847.1; -; mRNA.
DR EMBL; AB102720; BAD10848.1; -; mRNA.
DR EMBL; AB102721; BAD10849.1; -; mRNA.
DR EMBL; AB102722; BAD10850.1; -; mRNA.
DR EMBL; AK314485; BAG37088.1; -; mRNA.
DR EMBL; AB113249; BAD24805.1; -; mRNA.
DR EMBL; BX538033; CAD97978.1; -; mRNA.
DR EMBL; AL138759; CAD13191.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50035.1; -; Genomic_DNA.
DR EMBL; BC015477; AAH15477.1; -; mRNA.
DR EMBL; BC029381; AAH29381.1; ALT_INIT; mRNA.
DR EMBL; BC030963; AAH30963.1; ALT_INIT; mRNA.
DR EMBL; BC031004; AAH31004.1; ALT_INIT; mRNA.
DR EMBL; AY007108; AAG01987.1; ALT_INIT; mRNA.
DR EMBL; AB074174; BAE45737.1; -; mRNA.
DR RefSeq; NP_060533.2; NM_018063.3.
DR RefSeq; XP_005269782.1; XM_005269725.1.
DR RefSeq; XP_005269783.1; XM_005269726.1.
DR RefSeq; XP_005269784.1; XM_005269727.1.
DR RefSeq; XP_005269785.1; XM_005269728.1.
DR UniGene; Hs.655830; -.
DR ProteinModelPortal; Q9NRZ9; -.
DR SMR; Q9NRZ9; 214-486, 510-743.
DR IntAct; Q9NRZ9; 5.
DR MINT; MINT-2819086; -.
DR PhosphoSite; Q9NRZ9; -.
DR DMDM; 74761670; -.
DR PaxDb; Q9NRZ9; -.
DR PRIDE; Q9NRZ9; -.
DR DNASU; 3070; -.
DR Ensembl; ENST00000348459; ENSP00000239027; ENSG00000119969.
DR Ensembl; ENST00000394036; ENSP00000377601; ENSG00000119969.
DR Ensembl; ENST00000394044; ENSP00000377608; ENSG00000119969.
DR Ensembl; ENST00000394045; ENSP00000377609; ENSG00000119969.
DR GeneID; 3070; -.
DR KEGG; hsa:3070; -.
DR UCSC; uc001kjs.3; human.
DR CTD; 3070; -.
DR GeneCards; GC10P096305; -.
DR H-InvDB; HIX0017337; -.
DR HGNC; HGNC:4861; HELLS.
DR HPA; CAB004491; -.
DR MIM; 603946; gene.
DR neXtProt; NX_Q9NRZ9; -.
DR PharmGKB; PA35054; -.
DR eggNOG; COG0553; -.
DR HOVERGEN; HBG060049; -.
DR OrthoDB; EOG7TXKG5; -.
DR PhylomeDB; Q9NRZ9; -.
DR ChiTaRS; HELLS; human.
DR GeneWiki; HELLS; -.
DR GenomeRNAi; 3070; -.
DR NextBio; 12147; -.
DR PRO; PR:Q9NRZ9; -.
DR ArrayExpress; Q9NRZ9; -.
DR Bgee; Q9NRZ9; -.
DR Genevestigator; Q9NRZ9; -.
DR GO; GO:0005721; C:centromeric heterochromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031508; P:centromeric heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0046651; P:lymphocyte proliferation; ISS:UniProtKB.
DR GO; GO:0010216; P:maintenance of DNA methylation; ISS:UniProtKB.
DR GO; GO:0006346; P:methylation-dependent chromatin silencing; ISS:UniProtKB.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2_N; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Complete proteome; Developmental protein; Helicase;
KW Hydrolase; Mitosis; Nucleotide-binding; Nucleus; Polymorphism;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 838 Lymphoid-specific helicase.
FT /FTId=PRO_0000260051.
FT DOMAIN 235 403 Helicase ATP-binding.
FT DOMAIN 603 767 Helicase C-terminal.
FT NP_BIND 248 255 ATP (By similarity).
FT COILED 30 115 Potential.
FT MOTIF 354 357 DEAH box.
FT VAR_SEQ 1 16 Missing (in isoform 2).
FT /FTId=VSP_052224.
FT VAR_SEQ 124 129 VMRKKR -> GNFVCG (in isoform 9).
FT /FTId=VSP_052225.
FT VAR_SEQ 130 838 Missing (in isoform 9).
FT /FTId=VSP_052226.
FT VAR_SEQ 313 442 Missing (in isoform 6).
FT /FTId=VSP_052227.
FT VAR_SEQ 313 344 Missing (in isoform 3).
FT /FTId=VSP_052228.
FT VAR_SEQ 313 315 VRN -> IYL (in isoform 8).
FT /FTId=VSP_052229.
FT VAR_SEQ 316 838 Missing (in isoform 8).
FT /FTId=VSP_052230.
FT VAR_SEQ 345 442 Missing (in isoform 5).
FT /FTId=VSP_052231.
FT VAR_SEQ 345 345 H -> L (in isoform 7).
FT /FTId=VSP_052232.
FT VAR_SEQ 346 838 Missing (in isoform 7).
FT /FTId=VSP_052233.
FT VAR_SEQ 783 838 Missing (in isoform 4).
FT /FTId=VSP_052234.
FT VARIANT 616 616 H -> R (found in a renal cell carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_064720.
FT CONFLICT 136 136 Y -> F (in Ref. 4; CAD97978).
FT CONFLICT 646 646 D -> N (in Ref. 4; CAD97978).
FT CONFLICT 696 696 W -> C (in Ref. 7; AAH29381).
FT CONFLICT 702 702 L -> P (in Ref. 9; BAE45737).
SQ SEQUENCE 838 AA; 97074 MW; FE8C644C23F2526E CRC64;
MPAERPAGSG GSEAPAMVEQ LDTAVITPAM LEEEEQLEAA GLERERKMLE KARMSWDRES
TEIRYRRLQH LLEKSNIYSK FLLTKMEQQQ LEEQKKKEKL ERKKESLKVK KGKNSIDASE
EKPVMRKKRG REDESYNISE VMSKEEILSV AKKNKKENED ENSSSTNLCV EDLQKNKDSN
SIIKDRLSET VRQNTKFFFD PVRKCNGQPV PFQQPKHFTG GVMRWYQVEG MEWLRMLWEN
GINGILADEM GLGKTVQCIA TIALMIQRGV PGPFLVCGPL STLPNWMAEF KRFTPDIPTM
LYHGTQEERQ KLVRNIYKRK GTLQIHPVVI TSFEIAMRDR NALQHCYWKY LIVDEGHRIK
NMKCRLIREL KRFNADNKLL LTGTPLQNNL SELWSLLNFL LPDVFDDLKS FESWFDITSL
SETAEDIIAK EREQNVLHML HQILTPFLLR RLKSDVALEV PPKREVVVYA PLSKKQEIFY
TAIVNRTIAN MFGSSEKETI ELSPTGRPKR RTRKSINYSK IDDFPNELEK LISQIQPEVD
RERAVVEVNI PVESEVNLKL QNIMMLLRKC CNHPYLIEYP IDPVTQEFKI DEELVTNSGK
FLILDRMLPE LKKRGHKVLL FSQMTSMLDI LMDYCHLRDF NFSRLDGSMS YSEREKNMHS
FNTDPEVFIF LVSTRAGGLG INLTAADTVI IYDSDWNPQS DLQAQDRCHR IGQTKPVVVY
RLVTANTIDQ KIVERAAAKR KLEKLIIHKN HFKGGQSGLN LSKNFLDPKE LMELLKSRDY
EREIKGSREK VISDKDLELL LDRSDLIDQM NASGPIKEKM GIFKILENSE DSSPECLF
//
MIM
603946
*RECORD*
*FIELD* NO
603946
*FIELD* TI
*603946 HELICASE, LYMPHOID-SPECIFIC; HELLS
;;LSH;;
SWI/SNF-RELATED, MATRIX-ASSOCIATED, ACTIN-DEPENDENT REGULATOR OF CHROMATIN,
read moreSUBFAMILY A, MEMBER 6; SMARCA6;;
PROLIFERATION-ASSOCIATED SNF2-LIKE GENE; PASG
*FIELD* TX
CLONING
DNA helicases play a role in a number of processes involving DNA strand
separation, including replication, repair, recombination, and
transcription. Jarvis et al. (1996) identified a mouse gene encoding a
novel putative helicase. They designated the gene lsh, for
lymphoid-specific helicase, because Northern blot analysis revealed that
it was expressed specifically in mouse early thymocytes.
Using Northern blot analysis, Geiman et al. (1998) found that human
HELLS is expressed in testis and thymus, 2 tissues that are highly
active in DNA recombination.
GENE STRUCTURE
Geiman et al. (1998) determined that the mouse Hells gene contains at
least 18 exons and spans more than 26.6 kb.
MAPPING
By fluorescence in situ hybridization, Geiman et al. (1998) mapped the
HELLS gene to mouse chromosome 19, regions C3-D1, and human chromosome
10q23.3-q24.2. These 2 regions share homology of synteny.
ANIMAL MODEL
To explore the function of Lsh during lymphoid development or
activation, Geiman and Muegge (2000) deleted the Lsh gene by homologous
recombination in embryonic stem cells. Fetal liver cells from Lsh -/-
mice were used as a source of hematopoietic precursors to reconstitute
lymphoid development in Rag2 -/- mice. Lsh -/- (compared to Lsh +/+ or
+/-) chimeras showed a modest reduction in thymocyte numbers. The
findings demonstrated that Lsh is not obligatory for normal lymphoid
development but is essential for normal proliferation of peripheral T
lymphocytes.
Using homologous recombination, Sun et al. (2004) disrupted the Pasg
gene in mice by deleting exons 10, 11, and 12, which encode helicase
domains III, IV, and part of II. Disruption of the Pasg gene not only
led to genomic hypomethylation and reexpression of repressed genes, but
also to premature aging that was associated with decreased proliferation
and increased replicative senescence. An altered gene expression pattern
was observed, particularly in senescence-related genes such as
p16(Ink4a) (600160) and Bmi1 (164831).
De La Fuente et al. (2006) showed that Lsh deletion in female mice led
to severe oocyte loss and lack of ovarian follicle formation. During the
zygotene stage in oocytes of wildtype female embryos, Lsh was present at
heterochromatin domains, and at the mid-pachytene stage, Lsh exhibited a
diffuse nucleoplasmic pattern delineating chromatin along the entire
length of synapsed chromosomes. Oocytes from Lsh-knockout mice exhibited
demethylation of transposable elements and tandem repeats at pericentric
heterochromatin, as well as incomplete chromosome synapsis associated
with persistent Rad51 (179617) foci and H2ax (601772) phosphorylation.
Failure to load crossover-associated foci resulted in the generation of
nonexchange chromosomes. De La Fuente et al. (2006) concluded that LSH
has a critical role in epigenetic gene silencing and maintenance of
genomic stability during female meiosis. They stated that Lsh is
involved in de novo methylation in mouse embryonic stem cells through an
interaction with methyltransferases and that Lsh deletion in mice can be
perinatal lethal.
Using Lsh -/- mouse embryos, Xi et al. (2007) found that Lsh was
involved in normal control of Polycomb repressive complex (PRC)-mediated
gene silencing. Lsh associated with some Hox genes (e.g., HOXA7; 142950)
and regulated Dnmt3b (602900) binding, DNA methylation, and silencing of
Hox genes during development. Lsh associated with PRC1 components and
influenced PRC-mediated histone modifications. Xi et al. (2007)
concluded that LSH is part of a feedback loop that reinforces DNA
methylation and silencing of PRC targets.
*FIELD* RF
1. De La Fuente, R.; Baumann, C.; Fan, T.; Schmidtmann, A.; Dobrinski,
I.; Muegge, K.: Lsh is required for meiotic chromosome synapsis and
retrotransposon silencing in female germ cells. Nature Cell Biol. 8:
1448-1454, 2006.
2. Geiman, T. M.; Durum, S. K.; Muegge, K.: Characterization of gene
expression, genomic structure, and chromosomal localization of Hells
(Lsh). Genomics 54: 477-483, 1998.
3. Geiman, T. M.; Muegge, K.: Lsh, an SNF2/helicase family member,
is required for proliferation of mature T lymphocytes. Proc. Nat.
Acad. Sci. 97: 4772-4777, 2000.
4. Jarvis, C. D.; Geiman, T.; Vila-Storm, M. P.; Osipovich, O.; Akella,
U.; Candeias, S.; Nathan, I.; Durum, S. K.; Muegge, K.: A novel putative
helicase produced in early murine lymphocytes. Gene 169: 203-207,
1996.
5. Sun, L.-Q.; Lee, D. W.; Zhang, Q.; Xiao, W.; Raabe, E. H.; Meeker,
A.; Miao, D.; Huso, D. L.; Arceci, R. J.: Growth retardation and
premature aging phenotypes in mice with disruption of the SNF2-like
gene, PASG. Genes Dev. 18: 1035-1046, 2004.
6. Xi, S.; Zhu, H.; Xu, H.; Schmidtmann, A.; Geiman, T. M.; Muegge,
K.: Lsh controls Hox gene silencing during development. Proc. Nat.
Acad. Sci. 104: 14366-14371, 2007. Note: Erratum: Proc. Nat. Acad.
Sci. 104: 16389 only, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 3/21/2008
Patricia A. Hartz - updated: 4/3/2007
Patricia A. Hartz - updated: 8/17/2004
Victor A. McKusick - updated: 7/19/2000
*FIELD* CD
Rebekah S. Rasooly: 6/29/1999
*FIELD* ED
terry: 06/20/2012
mgross: 3/24/2008
terry: 3/21/2008
wwang: 4/5/2007
terry: 4/3/2007
mgross: 8/26/2004
terry: 8/17/2004
mcapotos: 7/20/2000
mcapotos: 7/19/2000
mcapotos: 7/17/2000
mcapotos: 7/11/2000
terry: 6/15/2000
jlewis: 7/1/1999
*RECORD*
*FIELD* NO
603946
*FIELD* TI
*603946 HELICASE, LYMPHOID-SPECIFIC; HELLS
;;LSH;;
SWI/SNF-RELATED, MATRIX-ASSOCIATED, ACTIN-DEPENDENT REGULATOR OF CHROMATIN,
read moreSUBFAMILY A, MEMBER 6; SMARCA6;;
PROLIFERATION-ASSOCIATED SNF2-LIKE GENE; PASG
*FIELD* TX
CLONING
DNA helicases play a role in a number of processes involving DNA strand
separation, including replication, repair, recombination, and
transcription. Jarvis et al. (1996) identified a mouse gene encoding a
novel putative helicase. They designated the gene lsh, for
lymphoid-specific helicase, because Northern blot analysis revealed that
it was expressed specifically in mouse early thymocytes.
Using Northern blot analysis, Geiman et al. (1998) found that human
HELLS is expressed in testis and thymus, 2 tissues that are highly
active in DNA recombination.
GENE STRUCTURE
Geiman et al. (1998) determined that the mouse Hells gene contains at
least 18 exons and spans more than 26.6 kb.
MAPPING
By fluorescence in situ hybridization, Geiman et al. (1998) mapped the
HELLS gene to mouse chromosome 19, regions C3-D1, and human chromosome
10q23.3-q24.2. These 2 regions share homology of synteny.
ANIMAL MODEL
To explore the function of Lsh during lymphoid development or
activation, Geiman and Muegge (2000) deleted the Lsh gene by homologous
recombination in embryonic stem cells. Fetal liver cells from Lsh -/-
mice were used as a source of hematopoietic precursors to reconstitute
lymphoid development in Rag2 -/- mice. Lsh -/- (compared to Lsh +/+ or
+/-) chimeras showed a modest reduction in thymocyte numbers. The
findings demonstrated that Lsh is not obligatory for normal lymphoid
development but is essential for normal proliferation of peripheral T
lymphocytes.
Using homologous recombination, Sun et al. (2004) disrupted the Pasg
gene in mice by deleting exons 10, 11, and 12, which encode helicase
domains III, IV, and part of II. Disruption of the Pasg gene not only
led to genomic hypomethylation and reexpression of repressed genes, but
also to premature aging that was associated with decreased proliferation
and increased replicative senescence. An altered gene expression pattern
was observed, particularly in senescence-related genes such as
p16(Ink4a) (600160) and Bmi1 (164831).
De La Fuente et al. (2006) showed that Lsh deletion in female mice led
to severe oocyte loss and lack of ovarian follicle formation. During the
zygotene stage in oocytes of wildtype female embryos, Lsh was present at
heterochromatin domains, and at the mid-pachytene stage, Lsh exhibited a
diffuse nucleoplasmic pattern delineating chromatin along the entire
length of synapsed chromosomes. Oocytes from Lsh-knockout mice exhibited
demethylation of transposable elements and tandem repeats at pericentric
heterochromatin, as well as incomplete chromosome synapsis associated
with persistent Rad51 (179617) foci and H2ax (601772) phosphorylation.
Failure to load crossover-associated foci resulted in the generation of
nonexchange chromosomes. De La Fuente et al. (2006) concluded that LSH
has a critical role in epigenetic gene silencing and maintenance of
genomic stability during female meiosis. They stated that Lsh is
involved in de novo methylation in mouse embryonic stem cells through an
interaction with methyltransferases and that Lsh deletion in mice can be
perinatal lethal.
Using Lsh -/- mouse embryos, Xi et al. (2007) found that Lsh was
involved in normal control of Polycomb repressive complex (PRC)-mediated
gene silencing. Lsh associated with some Hox genes (e.g., HOXA7; 142950)
and regulated Dnmt3b (602900) binding, DNA methylation, and silencing of
Hox genes during development. Lsh associated with PRC1 components and
influenced PRC-mediated histone modifications. Xi et al. (2007)
concluded that LSH is part of a feedback loop that reinforces DNA
methylation and silencing of PRC targets.
*FIELD* RF
1. De La Fuente, R.; Baumann, C.; Fan, T.; Schmidtmann, A.; Dobrinski,
I.; Muegge, K.: Lsh is required for meiotic chromosome synapsis and
retrotransposon silencing in female germ cells. Nature Cell Biol. 8:
1448-1454, 2006.
2. Geiman, T. M.; Durum, S. K.; Muegge, K.: Characterization of gene
expression, genomic structure, and chromosomal localization of Hells
(Lsh). Genomics 54: 477-483, 1998.
3. Geiman, T. M.; Muegge, K.: Lsh, an SNF2/helicase family member,
is required for proliferation of mature T lymphocytes. Proc. Nat.
Acad. Sci. 97: 4772-4777, 2000.
4. Jarvis, C. D.; Geiman, T.; Vila-Storm, M. P.; Osipovich, O.; Akella,
U.; Candeias, S.; Nathan, I.; Durum, S. K.; Muegge, K.: A novel putative
helicase produced in early murine lymphocytes. Gene 169: 203-207,
1996.
5. Sun, L.-Q.; Lee, D. W.; Zhang, Q.; Xiao, W.; Raabe, E. H.; Meeker,
A.; Miao, D.; Huso, D. L.; Arceci, R. J.: Growth retardation and
premature aging phenotypes in mice with disruption of the SNF2-like
gene, PASG. Genes Dev. 18: 1035-1046, 2004.
6. Xi, S.; Zhu, H.; Xu, H.; Schmidtmann, A.; Geiman, T. M.; Muegge,
K.: Lsh controls Hox gene silencing during development. Proc. Nat.
Acad. Sci. 104: 14366-14371, 2007. Note: Erratum: Proc. Nat. Acad.
Sci. 104: 16389 only, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 3/21/2008
Patricia A. Hartz - updated: 4/3/2007
Patricia A. Hartz - updated: 8/17/2004
Victor A. McKusick - updated: 7/19/2000
*FIELD* CD
Rebekah S. Rasooly: 6/29/1999
*FIELD* ED
terry: 06/20/2012
mgross: 3/24/2008
terry: 3/21/2008
wwang: 4/5/2007
terry: 4/3/2007
mgross: 8/26/2004
terry: 8/17/2004
mcapotos: 7/20/2000
mcapotos: 7/19/2000
mcapotos: 7/17/2000
mcapotos: 7/11/2000
terry: 6/15/2000
jlewis: 7/1/1999