SLN11_HUMAN
ID SLN11_HUMAN Reviewed; 901 AA.
AC Q7Z7L1; E1P643; Q8N3S8; Q8N762; Q8TEE0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Schlafen family member 11 {ECO:0000305};
DE EC=3.6.-.- {ECO:0000269|PubMed:29395061};
GN Name=SLFN11 {ECO:0000312|HGNC:HGNC:26633};
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 [LARGE SCALE MRNA], AND VARIANTS PHE-121 AND ASP-301.
RC TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-301.
RC TISSUE=Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-301.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-301.
RC TISSUE=Skin;
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 INDUCTION.
RX PubMed=20956525; DOI=10.1074/jbc.m110.151076;
RA Katsoulidis E., Mavrommatis E., Woodard J., Shields M.A., Sassano A.,
RA Carayol N., Sawicki K.T., Munshi H.G., Platanias L.C.;
RT "Role of interferon {alpha} (IFN{alpha})-inducible Schlafen-5 in regulation
RT of anchorage-independent growth and invasion of malignant melanoma cells.";
RL J. Biol. Chem. 285:40333-40341(2010).
RN [7]
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 [8]
RP FUNCTION, TRNA-BINDING, AND INDUCTION.
RX PubMed=23000900; DOI=10.1038/nature11433;
RA Li M., Kao E., Gao X., Sandig H., Limmer K., Pavon-Eternod M., Jones T.E.,
RA Landry S., Pan T., Weitzman M.D., David M.;
RT "Codon-usage-based inhibition of HIV protein synthesis by human schlafen
RT 11.";
RL Nature 491:125-128(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22927417; DOI=10.1073/pnas.1205943109;
RA Zoppoli G., Regairaz M., Leo E., Reinhold W.C., Varma S., Ballestrero A.,
RA Doroshow J.H., Pommier Y.;
RT "Putative DNA/RNA helicase Schlafen-11 (SLFN11) sensitizes cancer cells to
RT DNA-damaging agents.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:15030-15035(2012).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RPA1, AND MUTAGENESIS OF
RP LYS-605 AND ASP-668.
RX PubMed=26658330; DOI=10.15252/embr.201540964;
RA Mu Y., Lou J., Srivastava M., Zhao B., Feng X.H., Liu T., Chen J.,
RA Huang J.;
RT "SLFN11 inhibits checkpoint maintenance and homologous recombination
RT repair.";
RL EMBO Rep. 17:94-109(2016).
RN [11]
RP INDUCTION, AND INTERACTION WITH DHX9.
RX PubMed=26625211; DOI=10.18632/oncotarget.6413;
RA Nogales V., Reinhold W.C., Varma S., Martinez-Cardus A., Moutinho C.,
RA Moran S., Heyn H., Sebio A., Barnadas A., Pommier Y., Esteller M.;
RT "Epigenetic inactivation of the putative DNA/RNA helicase SLFN11 in human
RT cancer confers resistance to platinum drugs.";
RL Oncotarget 7:3084-3097(2016).
RN [12]
RP INDUCTION.
RX PubMed=28196596; DOI=10.1016/j.ccell.2017.01.006;
RA Gardner E.E., Lok B.H., Schneeberger V.E., Desmeules P., Miles L.A.,
RA Arnold P.K., Ni A., Khodos I., de Stanchina E., Nguyen T., Sage J.,
RA Campbell J.E., Ribich S., Rekhtman N., Dowlati A., Massion P.P.,
RA Rudin C.M., Poirier J.T.;
RT "Chemosensitive relapse in small cell lung cancer proceeds through an EZH2-
RT SLFN11 axis.";
RL Cancer Cell 31:286-299(2017).
RN [13]
RP INDUCTION.
RX PubMed=27440269; DOI=10.1158/1078-0432.ccr-16-1040;
RA Lok B.H., Gardner E.E., Schneeberger V.E., Ni A., Desmeules P.,
RA Rekhtman N., de Stanchina E., Teicher B.A., Riaz N., Powell S.N.,
RA Poirier J.T., Rudin C.M.;
RT "PARP inhibitor activity correlates with SLFN11 expression and demonstrates
RT synergy with temozolomide in small cell lung cancer.";
RL Clin. Cancer Res. 23:523-535(2017).
RN [14]
RP INDUCTION.
RX PubMed=28212573; DOI=10.18632/oncotarget.15338;
RA Allison Stewart C., Tong P., Cardnell R.J., Sen T., Li L., Gay C.M.,
RA Masrorpour F., Fan Y., Bara R.O., Feng Y., Ru Y., Fujimoto J., Kundu S.T.,
RA Post L.E., Yu K., Shen Y., Glisson B.S., Wistuba I., Heymach J.V.,
RA Gibbons D.L., Wang J., Byers L.A.;
RT "Dynamic variations in epithelial-to-mesenchymal transition (EMT), ATM, and
RT SLFN11 govern response to PARP inhibitors and cisplatin in small cell lung
RT cancer.";
RL Oncotarget 8:28575-28587(2017).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RPA1; MCM3 AND DHX9, AND
RP MUTAGENESIS OF GLU-669.
RX PubMed=29395061; DOI=10.1016/j.molcel.2018.01.012;
RA Murai J., Tang S.W., Leo E., Baechler S.A., Redon C.E., Zhang H.,
RA Al Abo M., Rajapakse V.N., Nakamura E., Jenkins L.M.M., Aladjem M.I.,
RA Pommier Y.;
RT "SLFN11 blocks stressed replication forks independently of ATR.";
RL Mol. Cell 69:371-384(2018).
CC -!- FUNCTION: Inhibitor of DNA replication that promotes cell death in
CC response to DNA damage (PubMed:22927417, PubMed:26658330,
CC PubMed:29395061). Acts as a guardian of the genome by killing cells
CC with defective replication (PubMed:29395061). Persistently blocks
CC stressed replication forks by opening chromatin across replication
CC initiation sites at stressed replication forks, possibly leading to
CC unwind DNA ahead of the MCM helicase and block fork progression,
CC ultimately leading to cell death (PubMed:29395061). Acts independently
CC of ATR (PubMed:29395061). Also acts as an interferon (IFN)-induced
CC antiviral protein which acts as an inhibitor of retrovirus protein
CC synthesis (PubMed:23000900). Specifically abrogates the production of
CC retroviruses such as human immunodeficiency virus 1 (HIV-1) by acting
CC as a specific inhibitor of the synthesis of retroviruses encoded
CC proteins in a codon-usage-dependent manner (PubMed:23000900). Binds to
CC tRNAs and exploits the unique viral codon bias towards A/T nucleotides
CC (PubMed:23000900). The exact inhibition mechanism is unclear: may
CC either sequester tRNAs, prevent their maturation via post-
CC transcriptional processing or may accelerate their deacylation
CC (PubMed:23000900). Does not inhibit reverse transcription, integration
CC or production and nuclear export of viral RNA (PubMed:23000900).
CC {ECO:0000269|PubMed:22927417, ECO:0000269|PubMed:23000900,
CC ECO:0000269|PubMed:26658330, ECO:0000269|PubMed:29395061}.
CC -!- SUBUNIT: Interacts with MCM3 (PubMed:29395061). Interacts with DHX9
CC (PubMed:26625211, PubMed:29395061). Interacts with RPA1
CC (PubMed:26658330, PubMed:29395061). {ECO:0000269|PubMed:26625211,
CC ECO:0000269|PubMed:26658330, ECO:0000269|PubMed:29395061}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22927417,
CC ECO:0000269|PubMed:26658330, ECO:0000269|PubMed:29395061}. Chromosome
CC {ECO:0000269|PubMed:26658330, ECO:0000269|PubMed:29395061}.
CC Note=Recruited to stressed replication forks carrying extended RPA
CC filaments (PubMed:29395061). Recruited to DNA damage sites via
CC interaction with RPA1 (PubMed:26658330, PubMed:29395061).
CC {ECO:0000269|PubMed:26658330, ECO:0000269|PubMed:29395061}.
CC -!- TISSUE SPECIFICITY: Exhibits a wider expression range in ovarian and
CC colon adenocarcinoma than in their corresponding healthy tissues.
CC {ECO:0000269|PubMed:22927417}.
CC -!- INDUCTION: Down-regulated in small cell lung cancer (SCLC) cells
CC resistant to PARP inhibitor drugs (PubMed:26625211, PubMed:28196596,
CC PubMed:27440269, PubMed:28212573). Up-regulated by type I interferons,
CC poly-IC and poly-dAdT (PubMed:20956525, PubMed:23000900).
CC {ECO:0000269|PubMed:20956525, ECO:0000269|PubMed:23000900,
CC ECO:0000269|PubMed:26625211, ECO:0000269|PubMed:27440269,
CC ECO:0000269|PubMed:28196596, ECO:0000269|PubMed:28212573}.
CC -!- MISCELLANEOUS: Dominant determinant of sensitivity to DNA-damaging
CC anticancer drugs: acts by mediating cell death in response to DNA
CC damage induced by anticancer drugs (PubMed:29395061). Down-regulated in
CC a number of chemoresistant tumors (PubMed:26625211, PubMed:28196596,
CC PubMed:27440269, PubMed:28212573). {ECO:0000269|PubMed:26625211,
CC ECO:0000269|PubMed:27440269, ECO:0000269|PubMed:28196596,
CC ECO:0000269|PubMed:28212573, ECO:0000269|PubMed:29395061}.
CC -!- SIMILARITY: Belongs to the Schlafen family. Subgroup III subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85010.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK074184; BAB85010.1; ALT_FRAME; mRNA.
DR EMBL; AK092241; BAC03835.1; -; mRNA.
DR EMBL; AL831964; CAD38606.2; -; mRNA.
DR EMBL; AC060766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80156.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80157.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80158.1; -; Genomic_DNA.
DR EMBL; BC052586; AAH52586.1; -; mRNA.
DR CCDS; CCDS11294.1; -.
DR RefSeq; NP_001098057.1; NM_001104587.1.
DR RefSeq; NP_001098058.1; NM_001104588.1.
DR RefSeq; NP_001098059.1; NM_001104589.1.
DR RefSeq; NP_001098060.1; NM_001104590.1.
DR RefSeq; NP_689483.3; NM_152270.3.
DR RefSeq; XP_005258125.1; XM_005258068.3.
DR RefSeq; XP_006722234.1; XM_006722171.3.
DR RefSeq; XP_011523767.1; XM_011525465.2.
DR RefSeq; XP_016880788.1; XM_017025299.1.
DR AlphaFoldDB; Q7Z7L1; -.
DR SMR; Q7Z7L1; -.
DR BioGRID; 124851; 363.
DR IntAct; Q7Z7L1; 10.
DR MINT; Q7Z7L1; -.
DR STRING; 9606.ENSP00000378067; -.
DR iPTMnet; Q7Z7L1; -.
DR PhosphoSitePlus; Q7Z7L1; -.
DR SwissPalm; Q7Z7L1; -.
DR BioMuta; SLFN11; -.
DR DMDM; 313104011; -.
DR EPD; Q7Z7L1; -.
DR jPOST; Q7Z7L1; -.
DR MassIVE; Q7Z7L1; -.
DR MaxQB; Q7Z7L1; -.
DR PaxDb; Q7Z7L1; -.
DR PeptideAtlas; Q7Z7L1; -.
DR PRIDE; Q7Z7L1; -.
DR ProteomicsDB; 69561; -.
DR Antibodypedia; 15596; 53 antibodies from 15 providers.
DR DNASU; 91607; -.
DR Ensembl; ENST00000308377.8; ENSP00000312402.4; ENSG00000172716.17.
DR Ensembl; ENST00000394566.5; ENSP00000378067.1; ENSG00000172716.17.
DR Ensembl; ENST00000685675.1; ENSP00000510787.1; ENSG00000172716.17.
DR GeneID; 91607; -.
DR KEGG; hsa:91607; -.
DR MANE-Select; ENST00000685675.1; ENSP00000510787.1; NM_001376007.1; NP_001362936.1.
DR UCSC; uc002hjg.5; human.
DR CTD; 91607; -.
DR DisGeNET; 91607; -.
DR GeneCards; SLFN11; -.
DR HGNC; HGNC:26633; SLFN11.
DR HPA; ENSG00000172716; Low tissue specificity.
DR MIM; 614953; gene.
DR neXtProt; NX_Q7Z7L1; -.
DR OpenTargets; ENSG00000172716; -.
DR PharmGKB; PA144596358; -.
DR VEuPathDB; HostDB:ENSG00000172716; -.
DR eggNOG; ENOG502QWKG; Eukaryota.
DR GeneTree; ENSGT00410000025651; -.
DR HOGENOM; CLU_007071_0_0_1; -.
DR InParanoid; Q7Z7L1; -.
DR OMA; ACMIRVK; -.
DR OrthoDB; 211385at2759; -.
DR PhylomeDB; Q7Z7L1; -.
DR TreeFam; TF337168; -.
DR PathwayCommons; Q7Z7L1; -.
DR SignaLink; Q7Z7L1; -.
DR BioGRID-ORCS; 91607; 17 hits in 1076 CRISPR screens.
DR ChiTaRS; SLFN11; human.
DR GeneWiki; SLFN11; -.
DR GenomeRNAi; 91607; -.
DR Pharos; Q7Z7L1; Tbio.
DR PRO; PR:Q7Z7L1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q7Z7L1; protein.
DR Bgee; ENSG00000172716; Expressed in monocyte and 139 other tissues.
DR ExpressionAtlas; Q7Z7L1; baseline and differential.
DR Genevisible; Q7Z7L1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
DR GO; GO:0043111; P:replication fork arrest; IDA:UniProtKB.
DR Gene3D; 3.30.950.30; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029684; Schlafen.
DR InterPro; IPR007421; Schlafen_AlbA_2_dom.
DR InterPro; IPR038461; Schlafen_AlbA_2_dom_sf.
DR InterPro; IPR018647; SLFN_3-like_DNA/RNA_helicase.
DR PANTHER; PTHR12155; PTHR12155; 1.
DR Pfam; PF04326; AlbA_2; 1.
DR Pfam; PF09848; DUF2075; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Chromosome; DNA damage; Helicase;
KW Hydrolase; Immunity; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding; tRNA-binding.
FT CHAIN 1..901
FT /note="Schlafen family member 11"
FT /id="PRO_0000283091"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 121
FT /note="V -> F (in dbSNP:rs12453150)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_031492"
FT VARIANT 301
FT /note="N -> D (in dbSNP:rs4796077)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.4"
FT /id="VAR_031493"
FT VARIANT 489
FT /note="R -> L (in dbSNP:rs9898983)"
FT /id="VAR_062186"
FT VARIANT 822
FT /note="Y -> C (in dbSNP:rs3803860)"
FT /id="VAR_031494"
FT MUTAGEN 605
FT /note="K->M: Abolishes ATPase activity without affecting
FT its role in DNA damage response; when associated with A-
FT 668."
FT /evidence="ECO:0000269|PubMed:26658330"
FT MUTAGEN 668
FT /note="D->A: Abolishes ATPase activity without affecting
FT its role in DNA damage response; when associated with M-
FT 605."
FT /evidence="ECO:0000269|PubMed:26658330"
FT MUTAGEN 669
FT /note="E->Q: Abolishes ATPase activity, leading to abolish
FT ability to inhibit DNA replication without affecting
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:29395061"
FT CONFLICT 20
FT /note="N -> S (in Ref. 1; BAC03835)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="M -> T (in Ref. 1; BAC03835)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="V -> M (in Ref. 2; CAD38606)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="I -> V (in Ref. 1; BAC03835 and 2; CAD38606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 901 AA; 102836 MW; 514FD89CB7C12E8D CRC64;
MEANQCPLVV EPSYPDLVIN VGEVTLGEEN RKKLQKIQRD QEKERVMRAA CALLNSGGGV
IRMAKKVEHP VEMGLDLEQS LRELIQSSDL QAFFETKQQG RCFYIFVKSW SSGPFPEDRS
VKPRLCSLSS SLYRRSETSV RSMDSREAFC FLKTKRKPKI LEEGPFHKIH KGVYQELPNS
DPADPNSDPA DLIFQKDYLE YGEILPFPES QLVEFKQFST KHFQEYVKRT IPEYVPAFAN
TGGGYLFIGV DDKSREVLGC AKENVDPDSL RRKIEQAIYK LPCVHFCQPQ RPITFTLKIV
NVLKRGELYG YACMIRVNPF CCAVFSEAPN SWIVEDKYVC SLTTEKWVGM MTDTDPDLLQ
LSEDFECQLS LSSGPPLSRP VYSKKGLEHK KELQQLLFSV PPGYLRYTPE SLWRDLISEH
RGLEELINKQ MQPFFRGILI FSRSWAVDLN LQEKPGVICD ALLIAQNSTP ILYTILREQD
AEGQDYCTRT AFTLKQKLVN MGGYTGKVCV RAKVLCLSPE SSAEALEAAV SPMDYPASYS
LAGTQHMEAL LQSLVIVLLG FRSLLSDQLG CEVLNLLTAQ QYEIFSRSLR KNRELFVHGL
PGSGKTIMAM KIMEKIRNVF HCEAHRILYV CENQPLRNFI SDRNICRAET RKTFLRENFE
HIQHIVIDEA QNFRTEDGDW YGKAKSITRR AKGGPGILWI FLDYFQTSHL DCSGLPPLSD
QYPREELTRI VRNADPIAKY LQKEMQVIRS NPSFNIPTGC LEVFPEAEWS QGVQGTLRIK
KYLTVEQIMT CVADTCRRFF DRGYSPKDVA VLVSTAKEVE HYKYELLKAM RKKRVVQLSD
ACDMLGDHIV LDSVRRFSGL ERSIVFGIHP RTADPAILPN VLICLASRAK QHLYIFPWGG
H
