SMAL1_HUMAN
ID SMAL1_HUMAN Reviewed; 954 AA.
AC Q9NZC9; A6NEH0; Q53R00; Q96AY1; Q9NXQ5; Q9UFH3; Q9UI93;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1;
DE EC=3.6.4.-;
DE AltName: Full=HepA-related protein;
DE Short=hHARP;
DE AltName: Full=Sucrose nonfermenting protein 2-like 1;
GN Name=SMARCAL1; Synonyms=HARP;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10857751; DOI=10.1006/geno.2000.6174;
RA Coleman M.A., Eisen J.A., Mohrenweiser H.W.;
RT "Cloning and characterization of HARP/SMARCAL1: a prokaryotic HepA-related
RT SNF2 helicase protein from human and mouse.";
RL Genomics 65:274-282(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS SIOD PRO-468;
RP ASN-548; LEU-579; TRP-586; TRP-644; CYS-645; GLN-647; THR-647; ILE-705;
RP GLN-764 AND HIS-820.
RX PubMed=11799392; DOI=10.1038/ng821;
RA Boerkoel C.F., Takashima H., John J., Yan J., Stankiewicz P.,
RA Rosenbarker L., Andre J.-L., Bogdanovic R., Burguet A., Cockfield S.,
RA Cordeiro I., Frund S., Illies F., Joseph M., Kaitila I., Lama G.,
RA Loirat C., McLeod D.R., Milford D.V., Petty E.M., Rodrigo F., Saraiva J.M.,
RA Schmidt B., Smith G.C., Spranger J., Stein A., Thiele H., Tizard J.,
RA Weksberg R., Lupski J.R., Stockton D.W.;
RT "Mutant chromatin remodeling protein SMARCAL1 causes Schimke immuno-osseous
RT dysplasia.";
RL Nat. Genet. 30:215-220(2002).
RN [3]
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-22 AND GLN-377.
RC TISSUE=Lung, and Lymph;
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 147-954.
RC TISSUE=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-954, AND VARIANT GLN-377.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9]
RP INTERACTION WITH RPA2 AND THE RPA COMPLEX, REGION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19793863; DOI=10.1101/gad.1831509;
RA Yusufzai T., Kong X., Yokomori K., Kadonaga J.T.;
RT "The annealing helicase HARP is recruited to DNA repair sites via an
RT interaction with RPA.";
RL Genes Dev. 23:2400-2404(2009).
RN [10]
RP FUNCTION IN DNA DAMAGE RESPONSE, INTERACTION WITH RPA2, AND
RP PHOSPHORYLATION.
RX PubMed=19793861; DOI=10.1101/gad.1839909;
RA Bansbach C.E., Betous R., Lovejoy C.A., Glick G.G., Cortez D.;
RT "The annealing helicase SMARCAL1 maintains genome integrity at stalled
RT replication forks.";
RL Genes Dev. 23:2405-2414(2009).
RN [11]
RP FUNCTION IN DNA REPLICATION, INTERACTION WITH RPA2 AND THE RPA COMPLEX,
RP REGION, SUBCELLULAR LOCATION, MUTAGENESIS OF 17-ARG--LYS-19, AND
RP CHARACTERIZATION OF VARIANTS SIOD TRP-586 AND GLN-764.
RX PubMed=19793862; DOI=10.1101/gad.1832309;
RA Ciccia A., Bredemeyer A.L., Sowa M.E., Terret M.E., Jallepalli P.V.,
RA Harper J.W., Elledge S.J.;
RT "The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved
RT in replication fork restart.";
RL Genes Dev. 23:2415-2425(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-123; SER-129 AND
RP SER-198, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, 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 [17]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-432.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [18]
RP CHARACTERIZATION OF VARIANTS SIOD TRP-586 AND GLN-764, FUNCTION, AND
RP DNA-BINDING.
RX PubMed=18974355; DOI=10.1126/science.1161233;
RA Yusufzai T., Kadonaga J.T.;
RT "HARP is an ATP-driven annealing helicase.";
RL Science 322:748-750(2008).
CC -!- FUNCTION: ATP-dependent annealing helicase that binds selectively to
CC fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the
CC stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably
CC bound by replication protein A (RPA). Acts throughout the genome to
CC reanneal stably unwound DNA, performing the opposite reaction of many
CC enzymes, such as helicases and polymerases, that unwind DNA. May play
CC an important role in DNA damage response by acting at stalled
CC replication forks. {ECO:0000269|PubMed:18974355,
CC ECO:0000269|PubMed:19793861, ECO:0000269|PubMed:19793862}.
CC -!- SUBUNIT: Interacts with RPA2; the interaction is direct and mediates
CC the recruitment by the RPA complex of SMARCAL1 to sites of DNA damage.
CC {ECO:0000269|PubMed:19793861, ECO:0000269|PubMed:19793862,
CC ECO:0000269|PubMed:19793863}.
CC -!- INTERACTION:
CC Q9NZC9; P15927: RPA2; NbExp=14; IntAct=EBI-5457961, EBI-621404;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19793862,
CC ECO:0000269|PubMed:19793863}. Note=Recruited to damaged DNA regions.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in testis.
CC {ECO:0000269|PubMed:10857751, ECO:0000269|PubMed:11799392}.
CC -!- PTM: DNA damage-regulated phosphorylation by kinases that may include
CC ATM, ATR and PRKDC. {ECO:0000269|PubMed:19793861}.
CC -!- DISEASE: Schimke immuno-osseous dysplasia (SIOD) [MIM:242900]: An
CC autosomal recessive pleiotropic disorder characterized by
CC spondyloepiphyseal dysplasia, renal dysfunction and immunodeficiency.
CC Arteriosclerosis may also occur in some case.
CC {ECO:0000269|PubMed:11799392, ECO:0000269|PubMed:18974355,
CC ECO:0000269|PubMed:19793862}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SMARCAL1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00800}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=SMARCAL1base; Note=SMARCAL1 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/SMARCAL1base/";
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DR EMBL; AF082179; AAF24984.1; -; mRNA.
DR EMBL; AF210842; AAF70454.1; -; Genomic_DNA.
DR EMBL; AF210833; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF210834; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF210835; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF210836; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF210837; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF210838; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF210839; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF210840; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF210841; AAF70454.1; JOINED; Genomic_DNA.
DR EMBL; AF432223; AAL73034.1; -; mRNA.
DR EMBL; AC098820; AAX93097.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70567.1; -; Genomic_DNA.
DR EMBL; BC016482; AAH16482.1; -; mRNA.
DR EMBL; BC043341; AAH43341.1; -; mRNA.
DR EMBL; AL122076; CAB59251.1; -; mRNA.
DR EMBL; AK000117; BAA90955.1; ALT_INIT; mRNA.
DR CCDS; CCDS2403.1; -.
DR PIR; T34557; T34557.
DR RefSeq; NP_001120679.1; NM_001127207.1.
DR RefSeq; NP_054859.2; NM_014140.3.
DR RefSeq; XP_005246688.1; XM_005246631.2.
DR RefSeq; XP_005246689.1; XM_005246632.1.
DR PDB; 4MQV; X-ray; 1.95 A; B/D=5-30.
DR PDBsum; 4MQV; -.
DR AlphaFoldDB; Q9NZC9; -.
DR SMR; Q9NZC9; -.
DR BioGRID; 119072; 33.
DR ELM; Q9NZC9; -.
DR IntAct; Q9NZC9; 16.
DR MINT; Q9NZC9; -.
DR STRING; 9606.ENSP00000349823; -.
DR GlyConnect; 2837; 1 N-Linked glycan (1 site).
DR GlyGen; Q9NZC9; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9NZC9; -.
DR MetOSite; Q9NZC9; -.
DR PhosphoSitePlus; Q9NZC9; -.
DR BioMuta; SMARCAL1; -.
DR DMDM; 60390962; -.
DR EPD; Q9NZC9; -.
DR jPOST; Q9NZC9; -.
DR MassIVE; Q9NZC9; -.
DR MaxQB; Q9NZC9; -.
DR PaxDb; Q9NZC9; -.
DR PeptideAtlas; Q9NZC9; -.
DR PRIDE; Q9NZC9; -.
DR ProteomicsDB; 83371; -.
DR Antibodypedia; 34237; 200 antibodies from 31 providers.
DR DNASU; 50485; -.
DR Ensembl; ENST00000357276.9; ENSP00000349823.4; ENSG00000138375.13.
DR Ensembl; ENST00000358207.9; ENSP00000350940.5; ENSG00000138375.13.
DR GeneID; 50485; -.
DR KEGG; hsa:50485; -.
DR MANE-Select; ENST00000357276.9; ENSP00000349823.4; NM_014140.4; NP_054859.2.
DR UCSC; uc002vgc.5; human.
DR CTD; 50485; -.
DR DisGeNET; 50485; -.
DR GeneCards; SMARCAL1; -.
DR GeneReviews; SMARCAL1; -.
DR HGNC; HGNC:11102; SMARCAL1.
DR HPA; ENSG00000138375; Low tissue specificity.
DR MalaCards; SMARCAL1; -.
DR MIM; 242900; phenotype.
DR MIM; 606622; gene.
DR neXtProt; NX_Q9NZC9; -.
DR OpenTargets; ENSG00000138375; -.
DR Orphanet; 1830; Schimke immuno-osseous dysplasia.
DR PharmGKB; PA35952; -.
DR VEuPathDB; HostDB:ENSG00000138375; -.
DR eggNOG; KOG1000; Eukaryota.
DR GeneTree; ENSGT00940000157608; -.
DR InParanoid; Q9NZC9; -.
DR OMA; QEEMPTA; -.
DR OrthoDB; 1082831at2759; -.
DR PhylomeDB; Q9NZC9; -.
DR TreeFam; TF106474; -.
DR PathwayCommons; Q9NZC9; -.
DR SignaLink; Q9NZC9; -.
DR BioGRID-ORCS; 50485; 27 hits in 1093 CRISPR screens.
DR ChiTaRS; SMARCAL1; human.
DR GeneWiki; SMARCAL1; -.
DR GenomeRNAi; 50485; -.
DR Pharos; Q9NZC9; Tbio.
DR PRO; PR:Q9NZC9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NZC9; protein.
DR Bgee; ENSG00000138375; Expressed in stromal cell of endometrium and 187 other tissues.
DR ExpressionAtlas; Q9NZC9; baseline and differential.
DR Genevisible; Q9NZC9; HS.
DR GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:CACAO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; IBA:GO_Central.
DR GO; GO:0090656; P:t-circle formation; TAS:BHF-UCL.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030101; HARP(SMARCAL1).
DR InterPro; IPR010003; HARP_dom.
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 PANTHER; PTHR45766:SF3; PTHR45766:SF3; 2.
DR Pfam; PF07443; HARP; 2.
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; PS51467; HARP; 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; ATP-binding; Coiled coil; Disease variant;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..954
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A-like protein 1"
FT /id="PRO_0000074348"
FT DOMAIN 226..303
FT /note="HARP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 327..398
FT /note="HARP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 445..600
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 716..869
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..30
FT /note="Mediates interaction with RPA2"
FT REGION 27..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..34
FT /evidence="ECO:0000255"
FT MOTIF 549..552
FT /note="DESH box"
FT COMPBIAS 32..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 458..465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 22
FT /note="A -> G (in dbSNP:rs17851400)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038370"
FT VARIANT 43
FT /note="A -> T (in dbSNP:rs2066524)"
FT /id="VAR_021363"
FT VARIANT 114
FT /note="R -> H (in dbSNP:rs11555797)"
FT /id="VAR_021364"
FT VARIANT 207
FT /note="I -> F (in dbSNP:rs6734114)"
FT /id="VAR_021366"
FT VARIANT 315
FT /note="S -> R (in dbSNP:rs2066522)"
FT /id="VAR_021367"
FT VARIANT 377
FT /note="E -> Q (in dbSNP:rs2066518)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_021368"
FT VARIANT 424
FT /note="D -> V (in dbSNP:rs2066520)"
FT /id="VAR_021369"
FT VARIANT 432
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036026"
FT VARIANT 468
FT /note="A -> P (in SIOD)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021370"
FT VARIANT 548
FT /note="I -> N (in SIOD; dbSNP:rs119473036)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021371"
FT VARIANT 579
FT /note="S -> L (in SIOD)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021372"
FT VARIANT 586
FT /note="R -> W (in SIOD; impairs without abolishing
FT annealing helicase activity; no effect on specific binding
FT to fork DNA; no effect on recruitment to sites of DNA
FT damage; dbSNP:rs119473038)"
FT /evidence="ECO:0000269|PubMed:11799392,
FT ECO:0000269|PubMed:18974355, ECO:0000269|PubMed:19793862"
FT /id="VAR_021373"
FT VARIANT 644
FT /note="R -> W (in SIOD; dbSNP:rs1313658611)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021374"
FT VARIANT 645
FT /note="R -> C (in SIOD; dbSNP:rs119473037)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021375"
FT VARIANT 647
FT /note="K -> Q (in SIOD)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021376"
FT VARIANT 647
FT /note="K -> T (in SIOD)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021377"
FT VARIANT 649
FT /note="D -> N (in dbSNP:rs2066523)"
FT /id="VAR_021378"
FT VARIANT 705
FT /note="T -> I (in SIOD; dbSNP:rs200644381)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021379"
FT VARIANT 742
FT /note="T -> M (in dbSNP:rs2271336)"
FT /id="VAR_021380"
FT VARIANT 764
FT /note="R -> Q (in SIOD; abolishes annealing helicase
FT activity; no effect on specific binding to fork DNA; no
FT effect on recruitment to sites of DNA damage;
FT dbSNP:rs267607071)"
FT /evidence="ECO:0000269|PubMed:11799392,
FT ECO:0000269|PubMed:18974355, ECO:0000269|PubMed:19793862"
FT /id="VAR_021381"
FT VARIANT 820
FT /note="R -> H (in SIOD; dbSNP:rs200666300)"
FT /evidence="ECO:0000269|PubMed:11799392"
FT /id="VAR_021382"
FT MUTAGEN 17..19
FT /note="RQK->AAA: Loss of interaction with RPA2 and impaired
FT recruitment by the RPA complex to sites of DNA damage."
FT /evidence="ECO:0000269|PubMed:19793862"
FT CONFLICT 118
FT /note="A -> T (in Ref. 1; AAF24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="C -> G (in Ref. 1; AAF24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="E -> K (in Ref. 7; BAA90955)"
FT /evidence="ECO:0000305"
FT CONFLICT 882
FT /note="I -> M (in Ref. 1; AAF24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="L -> V (in Ref. 1; AAF24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 911
FT /note="A -> G (in Ref. 1; AAF24984)"
FT /evidence="ECO:0000305"
FT HELIX 7..29
FT /evidence="ECO:0007829|PDB:4MQV"
SQ SEQUENCE 954 AA; 105938 MW; C5C762C24A2FDD3A CRC64;
MSLPLTEEQR KKIEENRQKA LARRAEKLLA EQHQRTSSGT SIAGNPFQAK QGPSQNFPRE
SCKPVSHGVI FKQQNLSSSS NADQRPHDSH SFQAKGIWKK PEEMPTACPG HSPRSQMALT
GISPPLAQSP PEVPKQQLLS YELGQGHAQA SPEIRFTPFA NPTHKPLAKP KSSQETPAHS
SGQPPRDAKL EAKTAKASPS GQNISYIHSS SESVTPRTEG RLQQKSGSSV QKGVNSQKGK
CVRNGDRFQV LIGYNAELIA VFKTLPSKNY DPDTKTWNFS MNDYSALMKA AQSLPTVNLQ
PLEWAYGSSE SPSTSSEGQA GLPSAPSLSF VKGRCMLISR AYFEADISYS QDLIALFKQM
DSRRYDVKTR KWSFLLEEHS KLIAKVRCLP QVQLDPLPTT LTLAFASQLK KTSLSLTPDV
PEADLSEVDP KLVSNLMPFQ RAGVNFAIAK GGRLLLADDM GLGKTIQAIC IAAFYRKEWP
LLVVVPSSVR FTWEQAFLRW LPSLSPDCIN VVVTGKDRLT AGLINIVSFD LLSKLEKQLK
TPFKVVIIDE SHFLKNSRTA RCRAAMPVLK VAKRVILLSG TPAMSRPAEL YTQIIAVKPT
FFPQFHAFGL RYCDAKRMPW GWDYSGSSNL GELKLLLEEA VMLRRLKSDV LSQLPAKQRK
IVVIAPGRIN ARTRAALDAA AKEMTTKDKT KQQQKDALIL FFNRTAEAKI PSVIEYILDL
LESGREKFLV FAHHKVVLDA ITQELERKHV QHIRIDGSTS SAEREDLCQQ FQLSERHAVA
VLSITAANMG LTFSSADLVV FAELFWNPGV LIQAEDRVHR IGQTSSVGIH YLVAKGTADD
YLWPLIQEKI KVLAEAGLSE TNFSEMTEST DYLYKDPKQQ KIYDLFQKSF EKEGSDMELL
EAAESFDPGS ASGTSGSSSQ NMGDTLDESS LTASPQKKRR FEFFDNWDSF TSPL
