ID HELLS_HUMAN Reviewed; 838 AA.
AC Q9NRZ9; B2RB41; Q3LID1; Q6I7N7; Q76H76; Q76H77; Q76H78; Q76H79; Q76H80;
AC Q76H81; Q7Z397; Q7Z5X2; Q8N6P4; Q9H4P5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 173.
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 {ECO:0000312|HGNC:HGNC:4861};
GN Synonyms=PASG {ECO:0000303|PubMed:10910076},
GN SMARCA6 {ECO:0000312|EMBL:AAF82262.1}; ORFNames=Nbla10143;
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] {ECO:0000305, ECO:0000312|EMBL:AAF82262.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND 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] {ECO:0000305, ECO:0000312|EMBL:BAD10846.1}
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., Kobayashi K.,
RA Inaki Y., Toyooka S., Tsukuda K., Shimizu N., Shimizu K.;
RT "Tumor-specific exon creation of the HELLS/SMARCA6 gene in non-small cell
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5] {ECO:0000312|EMBL:AL138759}
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., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., 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] {ECO:0000305, ECO:0000312|EMBL:CAD97978.1}
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 [7] {ECO:0000305, ECO:0000312|EMBL:AAH30963.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 415-838 (ISOFORMS 1/2/3).
RC TISSUE=Bone marrow {ECO:0000312|EMBL:AAH30963.1},
RC Prostate {ECO:0000312|EMBL:AAH29381.1}, and
RC Uterus {ECO:0000312|EMBL:AAH15477.1};
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 [8] {ECO:0000305, ECO:0000312|EMBL:CAD97978.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 464-838 (ISOFORMS 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] {ECO:0000305, ECO:0000312|EMBL:BAE45737.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 467-838 (ISOFORMS 1/2/3/5/6).
RC TISSUE=Neuroblastoma {ECO:0000269|PubMed:12880961};
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 the
RT 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 the
RT 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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP INVOLVEMENT IN ICF4, AND VARIANTS ICF4 ARG-699 AND LEU-801 DEL.
RX PubMed=26216346; DOI=10.1038/ncomms8870;
RA Thijssen P.E., Ito Y., Grillo G., Wang J., Velasco G., Nitta H., Unoki M.,
RA Yoshihara M., Suyama M., Sun Y., Lemmers R.J., de Greef J.C., Gennery A.,
RA Picco P., Kloeckener-Gruissem B., Guengoer T., Reisli I., Picard C.,
RA Kebaili K., Roquelaure B., Iwai T., Kondo I., Kubota T.,
RA van Ostaijen-Ten Dam M.M., van Tol M.J., Weemaes C., Francastel C.,
RA van der Maarel S.M., Sasaki H.;
RT "Mutations in CDCA7 and HELLS cause immunodeficiency-centromeric
RT instability-facial anomalies syndrome.";
RL Nat. Commun. 6:7870-7870(2015).
RN [16]
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., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Plays an essential role in normal development and survival.
CC Involved in regulation of the expansion or survival of lymphoid cells.
CC Required for de novo or maintenance DNA methylation. May control
CC silencing of the imprinted CDKN1C gene through DNA methylation. May
CC play a role in formation and organization of heterochromatin, implying
CC a functional role in the regulation of transcription and mitosis (By
CC similarity). {ECO:0000250|UniProtKB:Q60848}.
CC -!- INTERACTION:
CC Q9NRZ9; O00716: E2F3; NbExp=2; IntAct=EBI-1056215, EBI-765551;
CC Q9NRZ9-6; P55212: CASP6; NbExp=3; IntAct=EBI-12003732, EBI-718729;
CC Q9NRZ9-6; P06307: CCK; NbExp=3; IntAct=EBI-12003732, EBI-6624398;
CC Q9NRZ9-6; Q9H1H1: GTSF1L; NbExp=3; IntAct=EBI-12003732, EBI-19128683;
CC Q9NRZ9-6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12003732, EBI-21591415;
CC Q9NRZ9-6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12003732, EBI-16439278;
CC Q9NRZ9-6; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-12003732, EBI-5280197;
CC Q9NRZ9-6; P62826: RAN; NbExp=3; IntAct=EBI-12003732, EBI-286642;
CC Q9NRZ9-6; Q14140: SERTAD2; NbExp=3; IntAct=EBI-12003732, EBI-2822051;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Closely associated
CC with pericentric heterochromatin. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1 {ECO:0000269|PubMed:10910076};
CC IsoId=Q9NRZ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRZ9-2; Sequence=VSP_052224;
CC Name=3 {ECO:0000269|PubMed:15305370};
CC IsoId=Q9NRZ9-3; Sequence=VSP_052228;
CC Name=4 {ECO:0000269|PubMed:15305370};
CC IsoId=Q9NRZ9-4; Sequence=VSP_052234;
CC Name=5 {ECO:0000269|PubMed:15305370};
CC IsoId=Q9NRZ9-5; Sequence=VSP_052231;
CC Name=6 {ECO:0000269|PubMed:15305370};
CC IsoId=Q9NRZ9-6; Sequence=VSP_052227;
CC Name=7 {ECO:0000269|PubMed:15305370};
CC IsoId=Q9NRZ9-7; Sequence=VSP_052232, VSP_052233;
CC Name=8 {ECO:0000269|PubMed:15305370};
CC IsoId=Q9NRZ9-8; Sequence=VSP_052229, VSP_052230;
CC Name=9 {ECO:0000269|PubMed:15305370};
CC IsoId=Q9NRZ9-9; Sequence=VSP_052225, VSP_052226;
CC -!- TISSUE SPECIFICITY: Highly expressed in proliferative tissues such as
CC adult thymus and testis, and expressed at lower levels in uterus, small
CC intestine, colon, and peripheral blood mononuclear cells. Also
CC expressed in neoplastic cell lines including those derived from myeloid
CC and lymphoid leukemias. {ECO:0000269|PubMed:10910076}.
CC -!- INDUCTION: By concanavalin-A in peripheral blood leukocytes.
CC {ECO:0000269|PubMed:10910076}.
CC -!- DISEASE: Immunodeficiency-centromeric instability-facial anomalies
CC syndrome 4 (ICF4) [MIM:616911]: A rare disorder characterized by a
CC variable immunodeficiency resulting in recurrent infections, facial
CC anomalies, and branching of chromosomes 1, 9, and 16. Other variable
CC symptoms include growth retardation, failure to thrive, and psychomotor
CC retardation. Laboratory studies show limited hypomethylation of DNA in
CC a small fraction of the genome in some, but not all, patients.
CC {ECO:0000269|PubMed:26216346}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH29381.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH30963.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH31004.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS73163.1; -. [Q9NRZ9-5]
DR CCDS; CCDS7434.1; -. [Q9NRZ9-1]
DR CCDS; CCDS91306.1; -. [Q9NRZ9-3]
DR CCDS; CCDS91307.1; -. [Q9NRZ9-6]
DR CCDS; CCDS91308.1; -. [Q9NRZ9-2]
DR RefSeq; NP_001275996.1; NM_001289067.1.
DR RefSeq; NP_001275997.1; NM_001289068.1. [Q9NRZ9-2]
DR RefSeq; NP_001275998.1; NM_001289069.1. [Q9NRZ9-3]
DR RefSeq; NP_001275999.1; NM_001289070.1. [Q9NRZ9-5]
DR RefSeq; NP_001276000.1; NM_001289071.1.
DR RefSeq; NP_001276001.1; NM_001289072.1. [Q9NRZ9-6]
DR RefSeq; NP_001276002.1; NM_001289073.1.
DR RefSeq; NP_001276003.1; NM_001289074.1.
DR RefSeq; NP_001276004.1; NM_001289075.1.
DR RefSeq; NP_060533.2; NM_018063.4. [Q9NRZ9-1]
DR AlphaFoldDB; Q9NRZ9; -.
DR SMR; Q9NRZ9; -.
DR BioGRID; 109320; 173.
DR IntAct; Q9NRZ9; 50.
DR MINT; Q9NRZ9; -.
DR STRING; 9606.ENSP00000377601; -.
DR GlyGen; Q9NRZ9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NRZ9; -.
DR MetOSite; Q9NRZ9; -.
DR PhosphoSitePlus; Q9NRZ9; -.
DR BioMuta; HELLS; -.
DR DMDM; 74761670; -.
DR EPD; Q9NRZ9; -.
DR jPOST; Q9NRZ9; -.
DR MassIVE; Q9NRZ9; -.
DR MaxQB; Q9NRZ9; -.
DR PaxDb; 9606-ENSP00000377601; -.
DR PeptideAtlas; Q9NRZ9; -.
DR ProteomicsDB; 82450; -. [Q9NRZ9-1]
DR ProteomicsDB; 82451; -. [Q9NRZ9-2]
DR ProteomicsDB; 82452; -. [Q9NRZ9-3]
DR ProteomicsDB; 82453; -. [Q9NRZ9-4]
DR ProteomicsDB; 82454; -. [Q9NRZ9-5]
DR ProteomicsDB; 82455; -. [Q9NRZ9-6]
DR ProteomicsDB; 82456; -. [Q9NRZ9-7]
DR ProteomicsDB; 82457; -. [Q9NRZ9-8]
DR ProteomicsDB; 82458; -. [Q9NRZ9-9]
DR Pumba; Q9NRZ9; -.
DR Antibodypedia; 3852; 310 antibodies from 33 providers.
DR DNASU; 3070; -.
DR Ensembl; ENST00000348459.10; ENSP00000239027.7; ENSG00000119969.16. [Q9NRZ9-1]
DR Ensembl; ENST00000371332.9; ENSP00000360383.6; ENSG00000119969.16. [Q9NRZ9-9]
DR Ensembl; ENST00000394045.6; ENSP00000377609.1; ENSG00000119969.16. [Q9NRZ9-5]
DR Ensembl; ENST00000419900.6; ENSP00000409945.2; ENSG00000119969.16. [Q9NRZ9-2]
DR Ensembl; ENST00000698675.1; ENSP00000513940.1; ENSG00000119969.16. [Q9NRZ9-3]
DR Ensembl; ENST00000698799.1; ENSP00000513942.1; ENSG00000119969.16. [Q9NRZ9-6]
DR Ensembl; ENST00000698800.1; ENSP00000513943.1; ENSG00000119969.16. [Q9NRZ9-7]
DR Ensembl; ENST00000698830.1; ENSP00000513967.1; ENSG00000119969.16. [Q9NRZ9-8]
DR GeneID; 3070; -.
DR KEGG; hsa:3070; -.
DR MANE-Select; ENST00000348459.10; ENSP00000239027.7; NM_018063.5; NP_060533.2.
DR UCSC; uc001kjt.5; human. [Q9NRZ9-1]
DR AGR; HGNC:4861; -.
DR CTD; 3070; -.
DR DisGeNET; 3070; -.
DR GeneCards; HELLS; -.
DR HGNC; HGNC:4861; HELLS.
DR HPA; ENSG00000119969; Tissue enhanced (lymphoid).
DR MalaCards; HELLS; -.
DR MIM; 603946; gene.
DR MIM; 616911; phenotype.
DR neXtProt; NX_Q9NRZ9; -.
DR OpenTargets; ENSG00000119969; -.
DR Orphanet; 2268; ICF syndrome.
DR PharmGKB; PA35054; -.
DR VEuPathDB; HostDB:ENSG00000119969; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00740000115593; -.
DR InParanoid; Q9NRZ9; -.
DR OrthoDB; 5482994at2759; -.
DR PhylomeDB; Q9NRZ9; -.
DR TreeFam; TF329077; -.
DR PathwayCommons; Q9NRZ9; -.
DR SignaLink; Q9NRZ9; -.
DR BioGRID-ORCS; 3070; 20 hits in 1177 CRISPR screens.
DR ChiTaRS; HELLS; human.
DR GeneWiki; HELLS; -.
DR GenomeRNAi; 3070; -.
DR Pharos; Q9NRZ9; Tbio.
DR PRO; PR:Q9NRZ9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NRZ9; Protein.
DR Bgee; ENSG00000119969; Expressed in primordial germ cell in gonad and 146 other cell types or tissues.
DR ExpressionAtlas; Q9NRZ9; baseline and differential.
DR Genevisible; Q9NRZ9; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006306; P:DNA methylation; IBA:GO_Central.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0046651; P:lymphocyte proliferation; ISS:UniProtKB.
DR GO; GO:0044027; P:negative regulation of gene expression via CpG island methylation; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0031508; P:pericentric heterochromatin formation; ISS:UniProtKB.
DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
DR CDD; cd18009; DEXHc_HELLS_SMARCA6; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044753; HELLS_N.
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 PANTHER; PTHR47161; LYMPHOID-SPECIFIC HELICASE; 1.
DR PANTHER; PTHR47161:SF1; LYMPHOID-SPECIFIC HELICASE; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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; Coiled coil;
KW Developmental protein; Disease variant; Helicase; Hydrolase; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..838
FT /note="Lymphoid-specific helicase"
FT /id="PRO_0000260051"
FT DOMAIN 235..403
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 603..767
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 94..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 30..115
FT /evidence="ECO:0000255"
FT MOTIF 354..357
FT /note="DEAH box"
FT /evidence="ECO:0000255"
FT BINDING 248..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60848"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_052224"
FT VAR_SEQ 124..129
FT /note="VMRKKR -> GNFVCG (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052225"
FT VAR_SEQ 130..838
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052226"
FT VAR_SEQ 313..442
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052227"
FT VAR_SEQ 313..344
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052228"
FT VAR_SEQ 313..315
FT /note="VRN -> IYL (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052229"
FT VAR_SEQ 316..838
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052230"
FT VAR_SEQ 345..442
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052231"
FT VAR_SEQ 345
FT /note="H -> L (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052232"
FT VAR_SEQ 346..838
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052233"
FT VAR_SEQ 783..838
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15305370"
FT /id="VSP_052234"
FT VARIANT 616
FT /note="H -> R (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064720"
FT VARIANT 699
FT /note="Q -> R (in ICF4; uncertain significance;
FT dbSNP:rs879253733)"
FT /evidence="ECO:0000269|PubMed:26216346"
FT /id="VAR_076582"
FT VARIANT 801
FT /note="Missing (in ICF4; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:26216346"
FT /id="VAR_076583"
FT CONFLICT 136
FT /note="Y -> F (in Ref. 4; CAD97978)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="D -> N (in Ref. 4; CAD97978)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="W -> C (in Ref. 7; AAH29381)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="L -> P (in Ref. 9; BAE45737)"
FT /evidence="ECO:0000305"
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
//
