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HELLS_HUMAN
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   03-AUG-2022, entry version 164.
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   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; 157.
DR   IntAct; Q9NRZ9; 48.
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; Q9NRZ9; -.
DR   PeptideAtlas; Q9NRZ9; -.
DR   PRIDE; 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   Antibodypedia; 3852; 278 antibodies from 33 providers.
DR   DNASU; 3070; -.
DR   Ensembl; ENST00000348459.10; ENSP00000239027.7; ENSG00000119969.15. [Q9NRZ9-1]
DR   Ensembl; ENST00000394045.5; ENSP00000377609.1; ENSG00000119969.15. [Q9NRZ9-5]
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   CTD; 3070; -.
DR   DisGeNET; 3070; -.
DR   GeneCards; HELLS; -.
DR   HGNC; HGNC:4861; HELLS.
DR   HPA; ENSG00000119969; Tissue enhanced (bone marrow, lymphoid tissue).
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   PhylomeDB; Q9NRZ9; -.
DR   TreeFam; TF329077; -.
DR   PathwayCommons; Q9NRZ9; -.
DR   SignaLink; Q9NRZ9; -.
DR   BioGRID-ORCS; 3070; 18 hits in 1098 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 ventricular zone and 145 other 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 assembly; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; 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:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0031508; P:pericentric heterochromatin assembly; ISS:UniProtKB.
DR   CDD; cd18009; DEXHc_HELLS_SMARCA6; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
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; SSF52540; 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; unknown pathological significance;
FT                   dbSNP:rs879253733)"
FT                   /evidence="ECO:0000269|PubMed:26216346"
FT                   /id="VAR_076582"
FT   VARIANT         801
FT                   /note="Missing (in ICF4; unknown pathological
FT                   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
 
 
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