CTF18_HUMAN
ID CTF18_HUMAN Reviewed; 975 AA.
AC Q8WVB6; B7ZBA2; D3DU68; Q7Z6Y4; Q7Z6Y6; Q9BR83; Q9BRG5; Q9H7K3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Chromosome transmission fidelity protein 18 homolog;
DE Short=hCTF18;
DE AltName: Full=CHL12;
GN Name=CHTF18; Synonyms=C16orf41, CTF18;
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] (ISOFORM 3), AND VARIANTS PRO-82;
RP ARG-244 AND LEU-928.
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 GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Lung, and Placenta;
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 [5]
RP FUNCTION, IDENTIFICATION IN THE CTF18-RFC COMPLEX, INTERACTION WITH PCNA,
RP AND SUBCELLULAR LOCATION.
RX PubMed=12766176; DOI=10.1074/jbc.m211591200;
RA Merkle C.J., Karnitz L.M., Henry-Sanchez J.T., Chen J.;
RT "Cloning and characterization of hCTF18, hCTF8, and hDCC1. Human homologs
RT of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion
RT establishment.";
RL J. Biol. Chem. 278:30051-30056(2003).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE CTF18-RFC COMPLEX, INTERACTION WITH SMC1A
RP AND RAD21, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12930902; DOI=10.1073/pnas.1434308100;
RA Bermudez V.P., Maniwa Y., Tappin I., Ozato K., Yokomori K., Hurwitz J.;
RT "The alternative Ctf18-Dcc1-Ctf8-replication factor C complex required for
RT sister chromatid cohesion loads proliferating cell nuclear antigen onto
RT DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10237-10242(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-871, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP FUNCTION, AND INTERACTION WITH POLH.
RX PubMed=17545166; DOI=10.1074/jbc.m610102200;
RA Shiomi Y., Masutani C., Hanaoka F., Kimura H., Tsurimoto T.;
RT "A second proliferating cell nuclear antigen loader complex, Ctf18-
RT replication factor C, stimulates DNA polymerase eta activity.";
RL J. Biol. Chem. 282:20906-20914(2007).
RN [9]
RP IDENTIFICATION BY MASS 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 [10]
RP INTERACTION WITH DDX11.
RX PubMed=18499658; DOI=10.1074/jbc.m802696200;
RA Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S.,
RA Hurwitz J.;
RT "Studies with the human cohesin establishment factor, ChlR1. Association of
RT ChlR1 with Ctf18-RFC and Fen1.";
RL J. Biol. Chem. 283:20925-20936(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-871, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [15]
RP FUNCTION.
RX PubMed=20227374; DOI=10.1016/j.molcel.2010.02.009;
RA Ogi T., Limsirichaikul S., Overmeer R.M., Volker M., Takenaka K.,
RA Cloney R., Nakazawa Y., Niimi A., Miki Y., Jaspers N.G., Mullenders L.H.,
RA Yamashita S., Fousteri M.I., Lehmann A.R.;
RT "Three DNA polymerases, recruited by different mechanisms, carry out NER
RT repair synthesis in human cells.";
RL Mol. Cell 37:714-727(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, AND IDENTIFICATION BY
RP MASS 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; SER-64; SER-225 AND
RP SER-871, AND 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).
CC -!- FUNCTION: Chromosome cohesion factor involved in sister chromatid
CC cohesion and fidelity of chromosome transmission. Component of one of
CC the cell nuclear antigen loader complexes, CTF18-replication factor C
CC (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and
CC RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs
CC and has weak ATPase activity that is stimulated by the presence of
CC primed DNA, replication protein A (RPA) and by proliferating cell
CC nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-
CC dependent loading of PCNA onto primed and gapped DNA. Interacts with
CC and stimulates DNA polymerase POLH. During DNA repair synthesis,
CC involved in loading DNA polymerase POLE at the sites of local damage
CC (PubMed:20227374). {ECO:0000269|PubMed:12766176,
CC ECO:0000269|PubMed:12930902, ECO:0000269|PubMed:17545166,
CC ECO:0000269|PubMed:20227374}.
CC -!- SUBUNIT: Component of the CTF18-RFC complex, which consists of CTF18,
CC CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5 (PubMed:12766176,
CC PubMed:12930902). During assembly of the CTF18-RFC complex, CTF18 may
CC first assemble into a subcomplex with RFC2, RFC3, RFC4 and RFC5. CTF18
CC then interacts directly with CTF8, which in turn interacts with DCC1
CC (PubMed:12766176, PubMed:12930902). The CTF18-RFC complex associates
CC with PCNA and with DNA polymerase POLH (PubMed:12766176,
CC PubMed:17545166). The CTF18-RFC complex does not interact with the
CC Rad9/Rad1/Hus1 complex (PubMed:12766176). CTF18 interacts with SMC1A
CC and RAD21 (PubMed:12930902). Interacts with DDX11 (PubMed:18499658).
CC {ECO:0000269|PubMed:12766176, ECO:0000269|PubMed:12930902,
CC ECO:0000269|PubMed:17545166, ECO:0000269|PubMed:18499658}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12766176}.
CC Note=Associates with chromatin during S phase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WVB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVB6-2; Sequence=VSP_034180;
CC Name=3;
CC IsoId=Q8WVB6-3; Sequence=VSP_034179;
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. CTF18
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06437.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15766.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK024476; BAB15766.1; ALT_INIT; mRNA.
DR EMBL; AL031033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85706.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85707.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85711.1; -; Genomic_DNA.
DR EMBL; BC006278; AAH06278.2; -; mRNA.
DR EMBL; BC006437; AAH06437.1; ALT_INIT; mRNA.
DR EMBL; BC018184; AAH18184.1; -; mRNA.
DR CCDS; CCDS45371.1; -. [Q8WVB6-1]
DR RefSeq; NP_071375.1; NM_022092.2. [Q8WVB6-1]
DR RefSeq; XP_005255528.1; XM_005255471.3. [Q8WVB6-2]
DR RefSeq; XP_011520875.1; XM_011522573.1. [Q8WVB6-3]
DR AlphaFoldDB; Q8WVB6; -.
DR BioGRID; 121991; 87.
DR CORUM; Q8WVB6; -.
DR IntAct; Q8WVB6; 15.
DR MINT; Q8WVB6; -.
DR STRING; 9606.ENSP00000262315; -.
DR iPTMnet; Q8WVB6; -.
DR PhosphoSitePlus; Q8WVB6; -.
DR BioMuta; CHTF18; -.
DR DMDM; 74751544; -.
DR EPD; Q8WVB6; -.
DR jPOST; Q8WVB6; -.
DR MassIVE; Q8WVB6; -.
DR MaxQB; Q8WVB6; -.
DR PaxDb; Q8WVB6; -.
DR PeptideAtlas; Q8WVB6; -.
DR PRIDE; Q8WVB6; -.
DR ProteomicsDB; 74770; -. [Q8WVB6-1]
DR ProteomicsDB; 74771; -. [Q8WVB6-2]
DR ProteomicsDB; 74772; -. [Q8WVB6-3]
DR Antibodypedia; 5118; 179 antibodies from 26 providers.
DR DNASU; 63922; -.
DR Ensembl; ENST00000262315.14; ENSP00000262315.9; ENSG00000127586.17. [Q8WVB6-1]
DR Ensembl; ENST00000455171.6; ENSP00000406252.2; ENSG00000127586.17. [Q8WVB6-2]
DR GeneID; 63922; -.
DR KEGG; hsa:63922; -.
DR MANE-Select; ENST00000262315.14; ENSP00000262315.9; NM_022092.3; NP_071375.1.
DR UCSC; uc002cke.4; human. [Q8WVB6-1]
DR CTD; 63922; -.
DR DisGeNET; 63922; -.
DR GeneCards; CHTF18; -.
DR HGNC; HGNC:18435; CHTF18.
DR HPA; ENSG00000127586; Tissue enhanced (testis).
DR MIM; 613201; gene.
DR neXtProt; NX_Q8WVB6; -.
DR OpenTargets; ENSG00000127586; -.
DR PharmGKB; PA134908713; -.
DR VEuPathDB; HostDB:ENSG00000127586; -.
DR eggNOG; KOG1969; Eukaryota.
DR GeneTree; ENSGT00550000075029; -.
DR HOGENOM; CLU_004894_4_0_1; -.
DR InParanoid; Q8WVB6; -.
DR OMA; SYEDPMV; -.
DR OrthoDB; 307415at2759; -.
DR PhylomeDB; Q8WVB6; -.
DR TreeFam; TF314392; -.
DR PathwayCommons; Q8WVB6; -.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR SignaLink; Q8WVB6; -.
DR BioGRID-ORCS; 63922; 144 hits in 1085 CRISPR screens.
DR ChiTaRS; CHTF18; human.
DR GeneWiki; CHTF18; -.
DR GenomeRNAi; 63922; -.
DR Pharos; Q8WVB6; Tbio.
DR PRO; PR:Q8WVB6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8WVB6; protein.
DR Bgee; ENSG00000127586; Expressed in right testis and 116 other tissues.
DR ExpressionAtlas; Q8WVB6; baseline and differential.
DR Genevisible; Q8WVB6; HS.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; DNA replication;
KW DNA-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..975
FT /note="Chromosome transmission fidelity protein 18 homolog"
FT /id="PRO_0000340081"
FT REGION 30..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 374..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..418
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034179"
FT VAR_SEQ 95
FT /note="H -> HGRLAALPQGLRSGREAEEASGSLHVSPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034180"
FT VARIANT 63
FT /note="S -> F (in dbSNP:rs2277902)"
FT /id="VAR_043990"
FT VARIANT 82
FT /note="Q -> P (in dbSNP:rs2277901)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_043991"
FT VARIANT 244
FT /note="K -> R (in dbSNP:rs3765263)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_043992"
FT VARIANT 466
FT /note="A -> S (in dbSNP:rs34595992)"
FT /id="VAR_043993"
FT VARIANT 928
FT /note="P -> L (in dbSNP:rs2294451)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_043994"
SQ SEQUENCE 975 AA; 107383 MW; 1C71B8D71DA916CB CRC64;
MEDYEQELCG VEDDFHNQFA AELEVLAELE GASTPSPSGV PLFTAGRPPR TFEEALARGD
AASSPAPAAS VGSSQGGARK RQVDADLQPA GSLPHAPRIK RPRLQVVKRL NFRSEEMEEP
PPPDSSPTDI TPPPSPEDLA ELWGHGVSEA AADVGLTRAS PAARNPVLRR PPILEDYVHV
TSTEGVRAYL VLRADPMAPG VQGSLLHVPW RGGGQLDLLG VSLASLKKQV DGERRERLLQ
EAQKLSDTLH SLRSGEEEAA QPLGAPEEEP TDGQDASSHC LWVDEFAPRH YTELLSDDFT
NRCLLKWLKL WDLVVFGHER PSRKPRPSVE PARVSKEATA PGKWKSHEQV LEEMLEAGLD
PSQRPKQKVA LLCGPPGLGK TTLAHVIARH AGYSVVEMNA SDDRSPEVFR TRIEAATQME
SVLGAGGKPN CLVIDEIDGA PVAAINVLLS ILNRKGPQEV GPQGPAVPSG GGRRRRAEGG
LLMRPIICIC NDQFAPSLRQ LKQQAFLLHF PPTLPSRLVQ RLQEVSLRQG MRADPGVLAA
LCEKTDNDIR ACINTLQFLY SRGQRELSVR DVQATRVGLK DQRRGLFSVW QEVFQLPRAQ
RRRVGQDPAL PADTLLLGDG DAGSLTSASQ RFYRVLHAAA SAGEHEKVVQ GLFDNFLRLR
LRDSSLGAVC VALDWLAFDD LLAGAAHHSQ SFQLLRYPPF LPVAFHVLFA SSHTPRITFP
SSQQEAQNRM SQMRNLIQTL VSGIAPATRS RATPQALLLD ALCLLLDILA PKLRPVSTQL
YSTREKQQLA SLVGTMLAYS LTYRQERTPD GQYIYRLEPN VEELCRFPEL PARKPLTYQT
KQLIAREIEV EKMRRAEASA RVENSPQVDG SPPGLEGLLG GIGEKGVHRP APRNHEQRLE
HIMRRAAREE QPEKDFFGRV VVRSTAVPSA GDTAPEQDSV ERRMGTAVGR SEVWFRFNEG
VSNAVRRSLY IRDLL
