SMRCD_HUMAN
ID SMRCD_HUMAN Reviewed; 1026 AA.
AC Q9H4L7; B7Z799; Q05D56; Q96SX1; Q9H017; Q9H860; Q9NPU9; Q9ULU7;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase 1;
DE Short=hHEL1;
GN Name=SMARCAD1; Synonyms=KIAA1122;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP ALA-301.
RC TISSUE=Fetal brain;
RX PubMed=11031099; DOI=10.1006/geno.2000.6281;
RA Adra C.N., Donato J.-L., Badovinac R., Syed F., Kheraj R., Cai H.,
RA Moran C., Kolker M.T., Turner H., Weremowicz S., Shirakawa T., Morton C.C.,
RA Schnipper L.E., Drews R.;
RT "SMARCAD1, a novel human helicase family-defining member associated with
RT genetic instability: cloning, expression, and mapping to 4q22-q23, a band
RT rich in breakpoints and deletion mutants involved in several human
RT diseases.";
RL Genomics 69:162-173(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-702 (ISOFORMS 1/2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 649-1026 (ISOFORM 2).
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ASN-247;
RP ALA-301; GLN-351 AND ALA-972.
RC TISSUE=Kidney, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-1026 (ISOFORM 1).
RC TISSUE=Melanoma, and Testis;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-239 AND
RP SER-242, VARIANT [LARGE SCALE ANALYSIS] ASN-247, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-132 AND
RP SER-302, VARIANT [LARGE SCALE ANALYSIS] ALA-301, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP DNA-BINDING, AND INTERACTION WITH MSH2 AND TRIM28.
RX PubMed=18675275; DOI=10.1016/j.jmb.2008.07.031;
RA Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T.,
RA Ohara O., Koga H.;
RT "The novel protein complex with SMARCAD1/KIAA1122 binds to the vicinity of
RT TSS.";
RL J. Mol. Biol. 382:257-265(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-124; SER-127;
RP SER-132; SER-211 AND SER-214, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-124; SER-127; SER-132
RP AND SER-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-127, AND
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 INVOLVEMENT IN ADERM, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING (ISOFORM
RP 3).
RX PubMed=21820097; DOI=10.1016/j.ajhg.2011.07.004;
RA Nousbeck J., Burger B., Fuchs-Telem D., Pavlovsky M., Fenig S., Sarig O.,
RA Itin P., Sprecher E.;
RT "A mutation in a skin-specific isoform of SMARCAD1 causes autosomal-
RT dominant adermatoglyphia.";
RL Am. J. Hum. Genet. 89:302-307(2011).
RN [14]
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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PCNA; TRIM28; HDAC1;
RP HDAC2; EHMT2; PARP1 AND CBX3, AND MUTAGENESIS OF LYS-528.
RX PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
RA Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N.,
RA Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P.,
RA Mermoud J.E.;
RT "Maintenance of silent chromatin through replication requires SWI/SNF-like
RT chromatin remodeler SMARCAD1.";
RL Mol. Cell 42:285-296(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-57; SER-124; SER-127;
RP SER-146; SER-152; SER-239 AND SER-242, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22960744; DOI=10.1038/nature11353;
RA Costelloe T., Louge R., Tomimatsu N., Mukherjee B., Martini E.,
RA Khadaroo B., Dubois K., Wiegant W.W., Thierry A., Burma S., van Attikum H.,
RA Llorente B.;
RT "The yeast Fun30 and human SMARCAD1 chromatin remodellers promote DNA end
RT resection.";
RL Nature 489:581-584(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-79; SER-146; SER-152;
RP SER-211; SER-239 AND SER-302, VARIANT [LARGE SCALE ANALYSIS] ALA-301, 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 [21]
RP INVOLVEMENT IN BSNS.
RX PubMed=24664640; DOI=10.1002/ajmg.a.36438;
RA Marks K.C., Banks W.R. III, Cunningham D., Witman P.M., Herman G.E.;
RT "Analysis of two candidate genes for Basan syndrome.";
RL Am. J. Med. Genet. A 164A:1188-1191(2014).
RN [22]
RP INVOLVEMENT IN ADERM.
RX PubMed=24909267; DOI=10.1111/bjd.13176;
RA Nousbeck J., Sarig O., Magal L., Warshauer E., Burger B., Itin P.,
RA Sprecher E.;
RT "Mutations in SMARCAD1 cause autosomal dominant adermatoglyphia and perturb
RT the expression of epidermal differentiation-associated genes.";
RL Br. J. Dermatol. 171:1521-1524(2014).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-77, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [25]
RP INVOLVEMENT IN BSNS.
RX PubMed=26932190; DOI=10.1038/ejhg.2016.15;
RA Li M., Wang J., Li Z., Zhang J., Ni C., Cheng R., Yao Z.;
RT "Genome-wide linkage analysis and whole-genome sequencing identify a
RT recurrent SMARCAD1 variant in a unique Chinese family with Basan
RT syndrome.";
RL Eur. J. Hum. Genet. 24:1367-1370(2016).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-84; LYS-335; LYS-471;
RP LYS-724 AND LYS-996, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP INVOLVEMENT IN HRZ, AND TISSUE SPECIFICITY.
RX PubMed=29409814; DOI=10.1016/j.jid.2018.01.015;
RA Guenther C., Lee-Kirsch M.A., Eckhard J., Matanovic A., Kerscher T.,
RA Rueschendorf F., Klein B., Berndt N., Zimmermann N., Flachmeier C.,
RA Thuss T., Lucas N., Marenholz I., Esparza-Gordillo J., Huebner N.,
RA Traupe H., Delaporte E., Lee Y.A.;
RT "SMARCAD1 Haploinsufficiency Underlies Huriez Syndrome and Associated Skin
RT Cancer Susceptibility.";
RL J. Invest. Dermatol. 138:1428-1431(2018).
RN [28]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-301, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent
CC nucleosome-remodeling activity and is both required for DNA repair and
CC heterochromatin organization. Promotes DNA end resection of double-
CC strand breaks (DSBs) following DNA damage: probably acts by weakening
CC histone DNA interactions in nucleosomes flanking DSBs. Required for the
CC restoration of heterochromatin organization after replication. Acts at
CC replication sites to facilitate the maintenance of heterochromatin by
CC directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation
CC (H3K9me3) and restoration of silencing. {ECO:0000269|PubMed:21549307,
CC ECO:0000269|PubMed:22960744}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Binds to DNA preferentially in the vicinity of transcriptional
CC start sites. Interacts with MSH2 and TRIM28. Part of a complex composed
CC of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PCNA.
CC {ECO:0000269|PubMed:18675275, ECO:0000269|PubMed:21549307}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with PCNA
CC at replication forks during S phase. Recruited to double-strand breaks
CC (DSBs) sites of DNA damage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=Q9H4L7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4L7-2; Sequence=VSP_007104;
CC Name=3; Synonyms=Short;
CC IsoId=Q9H4L7-3; Sequence=VSP_043110;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed ubiquitously. Isoform 3 is
CC expressed mainly in skin and esophagus. Expressed in fibroblasts and
CC keratinocytes (at protein level) (PubMed:29409814).
CC {ECO:0000269|PubMed:11031099, ECO:0000269|PubMed:21820097,
CC ECO:0000269|PubMed:29409814}.
CC -!- DISEASE: Adermatoglyphia (ADERM) [MIM:136000]: An autosomal dominant
CC condition characterized by the lack of epidermal ridges on the palms
CC and soles, which results in the absence of fingerprints, and is
CC associated with a reduced number of sweat gland openings and reduced
CC sweating of palms and soles. {ECO:0000269|PubMed:21820097,
CC ECO:0000269|PubMed:24909267}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Splice site mutations
CC causing aberrant splicing of skin-specific isoform 3 are likely to
CC exert a loss-of-function effect and are involved in ADERM.
CC {ECO:0000269|PubMed:21820097, ECO:0000269|PubMed:24909267}.
CC -!- DISEASE: Basan syndrome (BSNS) [MIM:129200]: An autosomal dominant form
CC of adermatoglyphia associated with congenital facial milia, acral
CC blistering, digital contractures, and nail abnormalities.
CC Adermatoglyphia is defined by the lack of epidermal ridges on the palms
CC and soles, which results in the absence of fingerprints.
CC {ECO:0000269|PubMed:24664640, ECO:0000269|PubMed:26932190}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Splice site mutations causing aberrant splicing of skin-specific
CC isoform 3 are likely to exert a loss-of-function effect and are
CC involved in BSNS. {ECO:0000269|PubMed:24664640,
CC ECO:0000269|PubMed:26932190}.
CC -!- DISEASE: Huriez syndrome (HRZ) [MIM:181600]: An autosomal dominant
CC syndrome characterized by atrophic fibrosis of the skin of the limbs,
CC nail hypoplasia, and palmoplantar keratoderma. Malignant degeneration
CC of affected skin resulting in aggressive squamous cell carcinoma and
CC early metastasis formation is a distinctive feature of the syndrome.
CC {ECO:0000269|PubMed:29409814}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Skin-specific. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17953.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA86436.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14759.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The ends of our fingers
CC - Issue 136 of March 2012;
CC URL="https://web.expasy.org/spotlight/back_issues/136";
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DR EMBL; AY008271; AAG16639.1; -; mRNA.
DR EMBL; AB032948; BAA86436.2; ALT_INIT; mRNA.
DR EMBL; AK023990; BAB14759.1; ALT_INIT; mRNA.
DR EMBL; AK027490; BAB55150.1; -; mRNA.
DR EMBL; AK301668; BAH13535.1; -; mRNA.
DR EMBL; AC096746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017953; AAH17953.1; ALT_SEQ; mRNA.
DR EMBL; BC045534; AAH45534.1; -; mRNA.
DR EMBL; AL359929; CAB95769.1; -; mRNA.
DR EMBL; AL512768; CAC21685.1; -; mRNA.
DR CCDS; CCDS3639.1; -. [Q9H4L7-1]
DR CCDS; CCDS47101.1; -. [Q9H4L7-2]
DR CCDS; CCDS58914.1; -. [Q9H4L7-3]
DR RefSeq; NP_001121901.1; NM_001128429.2. [Q9H4L7-2]
DR RefSeq; NP_001121902.1; NM_001128430.1. [Q9H4L7-2]
DR RefSeq; NP_001241878.1; NM_001254949.1. [Q9H4L7-3]
DR RefSeq; NP_064544.2; NM_020159.4. [Q9H4L7-1]
DR RefSeq; XP_016863952.1; XM_017008463.1.
DR PDB; 6H3A; X-ray; 5.50 A; B/D=95-347.
DR PDB; 6QU1; X-ray; 3.70 A; D=151-198.
DR PDBsum; 6H3A; -.
DR PDBsum; 6QU1; -.
DR AlphaFoldDB; Q9H4L7; -.
DR SMR; Q9H4L7; -.
DR BioGRID; 121244; 174.
DR IntAct; Q9H4L7; 20.
DR MINT; Q9H4L7; -.
DR STRING; 9606.ENSP00000351947; -.
DR GlyGen; Q9H4L7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H4L7; -.
DR MetOSite; Q9H4L7; -.
DR PhosphoSitePlus; Q9H4L7; -.
DR BioMuta; SMARCAD1; -.
DR DMDM; 306526240; -.
DR EPD; Q9H4L7; -.
DR jPOST; Q9H4L7; -.
DR MassIVE; Q9H4L7; -.
DR MaxQB; Q9H4L7; -.
DR PaxDb; Q9H4L7; -.
DR PeptideAtlas; Q9H4L7; -.
DR PRIDE; Q9H4L7; -.
DR ProteomicsDB; 80860; -. [Q9H4L7-1]
DR ProteomicsDB; 80861; -. [Q9H4L7-2]
DR ProteomicsDB; 80862; -. [Q9H4L7-3]
DR Antibodypedia; 14709; 141 antibodies from 26 providers.
DR DNASU; 56916; -.
DR Ensembl; ENST00000354268.9; ENSP00000346217.4; ENSG00000163104.18. [Q9H4L7-1]
DR Ensembl; ENST00000359052.8; ENSP00000351947.4; ENSG00000163104.18. [Q9H4L7-2]
DR Ensembl; ENST00000457823.6; ENSP00000415576.2; ENSG00000163104.18. [Q9H4L7-2]
DR Ensembl; ENST00000509418.1; ENSP00000423286.1; ENSG00000163104.18. [Q9H4L7-3]
DR GeneID; 56916; -.
DR KEGG; hsa:56916; -.
DR MANE-Select; ENST00000354268.9; ENSP00000346217.4; NM_020159.5; NP_064544.2.
DR UCSC; uc003htb.5; human. [Q9H4L7-1]
DR CTD; 56916; -.
DR DisGeNET; 56916; -.
DR GeneCards; SMARCAD1; -.
DR HGNC; HGNC:18398; SMARCAD1.
DR HPA; ENSG00000163104; Low tissue specificity.
DR MalaCards; SMARCAD1; -.
DR MIM; 129200; phenotype.
DR MIM; 136000; phenotype.
DR MIM; 181600; phenotype.
DR MIM; 612761; gene.
DR neXtProt; NX_Q9H4L7; -.
DR OpenTargets; ENSG00000163104; -.
DR Orphanet; 1658; Absence of fingerprints-congenital milia syndrome.
DR Orphanet; 384; Huriez syndrome.
DR Orphanet; 289465; Isolated congenital adermatoglyphia.
DR PharmGKB; PA134954731; -.
DR VEuPathDB; HostDB:ENSG00000163104; -.
DR eggNOG; KOG0389; Eukaryota.
DR GeneTree; ENSGT00910000144252; -.
DR HOGENOM; CLU_000315_16_3_1; -.
DR InParanoid; Q9H4L7; -.
DR OMA; HNKYEDY; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q9H4L7; -.
DR TreeFam; TF105768; -.
DR PathwayCommons; Q9H4L7; -.
DR SignaLink; Q9H4L7; -.
DR SIGNOR; Q9H4L7; -.
DR BioGRID-ORCS; 56916; 13 hits in 1092 CRISPR screens.
DR ChiTaRS; SMARCAD1; human.
DR GeneWiki; SMARCAD1; -.
DR GenomeRNAi; 56916; -.
DR Pharos; Q9H4L7; Tbio.
DR PRO; PR:Q9H4L7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9H4L7; protein.
DR Bgee; ENSG00000163104; Expressed in adrenal tissue and 173 other tissues.
DR ExpressionAtlas; Q9H4L7; baseline and differential.
DR Genevisible; Q9H4L7; HS.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0043596; C:nuclear replication fork; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IMP:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IMP:GO_Central.
DR GO; GO:0051304; P:chromosome separation; IMP:UniProtKB.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:UniProtKB.
DR GO; GO:0070932; P:histone H3 deacetylation; IMP:UniProtKB.
DR GO; GO:0070933; P:histone H4 deacetylation; IMP:UniProtKB.
DR GO; GO:0000018; P:regulation of DNA recombination; IEP:UniProtKB.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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; PS51140; CUE; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Chromatin regulator; Chromosome; DNA damage; DNA repair; DNA-binding;
KW Ectodermal dysplasia; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Palmoplantar keratoderma; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1026
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A containing DEAD/H box 1"
FT /id="PRO_0000074356"
FT DOMAIN 157..199
FT /note="CUE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 251..294
FT /note="CUE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 509..677
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 858..1010
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 628..631
FT /note="DEGH box"
FT MOTIF 721..738
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1005..1008
FT /note="DEGD box"
FT COMPBIAS 44..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 897..904
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 217
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 471
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 996
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..430
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043110"
FT VAR_SEQ 765
FT /note="L -> LVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574461,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_007104"
FT VARIANT 66
FT /note="S -> F (in dbSNP:rs11723410)"
FT /id="VAR_028037"
FT VARIANT 135
FT /note="L -> F (in dbSNP:rs2664891)"
FT /id="VAR_028038"
FT VARIANT 140
FT /note="R -> C (in dbSNP:rs2632398)"
FT /id="VAR_028039"
FT VARIANT 245
FT /note="S -> Y (in dbSNP:rs3103117)"
FT /id="VAR_028040"
FT VARIANT 247
FT /note="S -> N (in dbSNP:rs11722476)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0007744|PubMed:17081983"
FT /id="VAR_028041"
FT VARIANT 301
FT /note="V -> A (in dbSNP:rs7439869)"
FT /evidence="ECO:0000269|PubMed:11031099,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:23186163"
FT /id="VAR_028042"
FT VARIANT 351
FT /note="P -> Q (in dbSNP:rs17854344)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028043"
FT VARIANT 972
FT /note="V -> A (in dbSNP:rs17857297)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028044"
FT MUTAGEN 528
FT /note="K->R: No effect on subcellular localization and on
FT histone deacetylation."
FT /evidence="ECO:0000269|PubMed:21549307"
FT CONFLICT 215
FT /note="E -> D (in Ref. 5; AAH17953)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="N -> D (in Ref. 3; BAB14759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1026 AA; 117402 MW; 0A5DB5653F478413 CRC64;
MNLFNLDRFR FEKRNKIEEA PEATPQPSQP GPSSPISLSA EEENAEGEVS RANTPDSDIT
EKTEDSSVPE TPDNERKASI SYFKNQRGIQ YIDLSSDSED VVSPNCSNTV QEKTFNKDTV
IIVSEPSEDE ESQGLPTMAR RNDDISELED LSELEDLKDA KLQTLKELFP QRSDNDLLKL
IESTSTMDGA IAAALLMFGD AGGGPRKRKL SSSSEPYEED EFNDDQSIKK TRLDHGEESN
ESAESSSNWE KQESIVLKLQ KEFPNFDKQE LREVLKEHEW MYTEALESLK VFAEDQDMQY
VSQSEVPNGK EVSSRSQNYP KNATKTKLKQ KFSMKAQNGF NKKRKKNVFN PKRVVEDSEY
DSGSDVGSSL DEDYSSGEEV MEDGYKGKIL HFLQDASIGE LTLIPQCSQK KAQKITELRP
FNSWEALFTK MSKTNGLSED LIWHCKTLIQ ERDVVIRLMN KCEDISNKLT KQVTMLTGNG
GGWNIEQPSI LNQSLSLKPY QKVGLNWLAL VHKHGLNGIL ADEMGLGKTI QAIAFLAYLY
QEGNNGPHLI VVPASTIDNW LREVNLWCPT LKVLCYYGSQ EERKQIRFNI HSRYEDYNVI
VTTYNCAISS SDDRSLFRRL KLNYAIFDEG HMLKNMGSIR YQHLMTINAN NRLLLTGTPV
QNNLLELMSL LNFVMPHMFS SSTSEIRRMF SSKTKSADEQ SIYEKERIAH AKQIIKPFIL
RRVKEEVLKQ LPPKKDRIEL CAMSEKQEQL YLGLFNRLKK SINNLEKNTE MCNVMMQLRK
MANHPLLHRQ YYTAEKLKEM SQLMLKEPTH CEANPDLIFE DMEVMTDFEL HVLCKQYRHI
NNFQLDMDLI LDSGKFRVLG CILSELKQKG DRVVLFSQFT MMLDILEVLL KHHQHRYLRL
DGKTQISERI HLIDEFNTDM DIFVFLLSTK AGGLGINLTS ANVVILHDID CNPYNDKQAE
DRCHRVGQTK EVLVIKLISQ GTIEESMLKI NQQKLKLEQD MTTVDEGDEG SMPADIATLL
KTSMGL
