ID CDC45_HUMAN Reviewed; 566 AA. AC O75419; B4DDB4; B4DDU3; E9PDH7; O60856; Q20WK8; Q6UW54; Q9UP68; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-NOV-2024, entry version 202. DE RecName: Full=Cell division control protein 45 homolog; DE AltName: Full=PORC-PI-1; GN Name=CDC45 {ECO:0000312|HGNC:HGNC:1739}; Synonyms=CDC45L, CDC45L2; GN ORFNames=UNQ374/PRO710; 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). RX PubMed=9755170; DOI=10.1093/emboj/17.19.5699; RA Mimura S., Takisawa H.; RT "Xenopus Cdc45-dependent loading of DNA polymerase alpha onto chromatin RT under the control of S-phase Cdk."; RL EMBO J. 17:5699-5707(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9660782; DOI=10.1074/jbc.273.29.18205; RA Saha P., Thome K.C., Yamaguchi R., Hou Z.-H., Weremowicz S., Dutta A.; RT "The human homolog of Saccharomyces cerevisiae CDC45."; RL J. Biol. Chem. 273:18205-18209(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9724329; DOI=10.1101/gr.8.8.834; RA McKie J.M., Wadey R.B., Sutherland H.F., Taylor C.L., Scambler P.J.; RT "Direct selection of conserved cDNAs from the DiGeorge critical region: RT isolation of a novel CDC45-like gene."; RL Genome Res. 8:834-841(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10051334; DOI=10.1007/s003359900996; RA Shaikh T.H., Gottlieb S., Sellinger B., Chen F., Roe B.A., Oakey R.J., RA Emanuel B.S., Budarf M.L.; RT "Characterization of CDC45L: a gene in the 22q11.2 deletion region RT expressed during murine and human development."; RL Mamm. Genome 10:322-326(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-81 AND MET-376. RG NIEHS SNPs program; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [11] 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 [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Muscle; 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-130; SER-144 AND SER-148, AND 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 [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 IDENTIFICATION BY MASS 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 [16] RP FUNCTION, AND INTERACTION WITH HELB. RX PubMed=25933514; DOI=10.1016/j.yexcr.2015.04.014; RA Gerhardt J., Guler G.D., Fanning E.; RT "Human DNA helicase B interacts with the replication initiation protein RT Cdc45 and facilitates Cdc45 binding onto chromatin."; RL Exp. Cell Res. 334:283-293(2015). RN [17] RP FUNCTION. RX PubMed=35585232; DOI=10.1038/s41586-022-04759-1; RA Baris Y., Taylor M.R.G., Aria V., Yeeles J.T.P.; RT "Fast and efficient DNA replication with purified human proteins."; RL Nature 606:204-210(2022). RN [18] {ECO:0007744|PDB:6XTX, ECO:0007744|PDB:6XTY} RP STRUCTURE BY ELECTRON MICROSCOPY (3.29 ANGSTROMS) IN CMG COMPLEX, SUBUNIT, RP AND FUNCTION. RX PubMed=32453425; DOI=10.1093/nar/gkaa429; RA Rzechorzek N.J., Hardwick S.W., Jatikusumo V.A., Chirgadze D.Y., RA Pellegrini L.; RT "CryoEM structures of human CMG-ATPgammaS-DNA and CMG-AND-1 complexes."; RL Nucleic Acids Res. 48:6980-6995(2020). RN [19] {ECO:0007744|PDB:7PFO} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) IN REPLISOME, SUBUNIT, RP AND FUNCTION. RX PubMed=34694004; DOI=10.15252/embj.2021108819; RA Jones M.L., Baris Y., Taylor M.R.G., Yeeles J.T.P.; RT "Structure of a human replisome shows the organisation and interactions of RT a DNA replication machine."; RL EMBO J. 40:e108819-e108819(2021). RN [20] {ECO:0007744|PDB:7PLO} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN REPLISOME, SUBUNIT, RP AND FUNCTION. RX PubMed=34700328; DOI=10.1038/s41586-021-04145-3; RA Jenkyn-Bedford M., Jones M.L., Baris Y., Labib K.P.M., Cannone G., RA Yeeles J.T.P., Deegan T.D.; RT "A conserved mechanism for regulating replisome disassembly in RT eukaryotes."; RL Nature 600:743-747(2021). RN [21] RP INVOLVEMENT IN MGORS7, VARIANTS MGORS7 ARG-68; HIS-76; GLY-155; CYS-157; RP GLY-226; TYR-264; VAL-298; THR-321; 424-ARG--SER-566 DEL; LEU-463; LEU-496 RP AND TRP-554, AND CHARACTERIZATION OF VARIANTS MGORS7 ARG-68; HIS-76; RP CYS-157; GLY-226 AND VAL-298. RX PubMed=27374770; DOI=10.1016/j.ajhg.2016.05.019; RG WGS500 Consortium; RA Fenwick A.L., Kliszczak M., Cooper F., Murray J., Sanchez-Pulido L., RA Twigg S.R., Goriely A., McGowan S.J., Miller K.A., Taylor I.B., Logan C., RA Bozdogan S., Danda S., Dixon J., Elsayed S.M., Elsobky E., Gardham A., RA Hoffer M.J., Koopmans M., McDonald-McGinn D.M., Santen G.W., RA Savarirayan R., de Silva D., Vanakker O., Wall S.A., Wilson L.C., RA Yuregir O.O., Zackai E.H., Ponting C.P., Jackson A.P., Wilkie A.O., RA Niedzwiedz W., Bicknell L.S.; RT "Mutations in CDC45, encoding an essential component of the pre-initiation RT complex, cause Meier-Gorlin syndrome and craniosynostosis."; RL Am. J. Hum. Genet. 99:125-138(2016). CC -!- FUNCTION: Required for initiation of chromosomal DNA replication. Core CC component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that CC unwinds template DNA during replication, and around which the replisome CC is built. {ECO:0000269|PubMed:32453425, ECO:0000269|PubMed:34694004, CC ECO:0000269|PubMed:34700328, ECO:0000269|PubMed:35585232}. CC -!- SUBUNIT: Component of the CMG helicase complex, a hexameric ring of CC related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS CC complex (PubMed:32453425, PubMed:34694004, PubMed:34700328). Associated CC with ORC2. Interacts with HELB (PubMed:25933514). CC {ECO:0000269|PubMed:25933514, ECO:0000269|PubMed:32453425, CC ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:34700328}. CC -!- INTERACTION: CC O75419; P38936: CDKN1A; NbExp=2; IntAct=EBI-374969, EBI-375077; CC O75419; Q53EZ4: CEP55; NbExp=7; IntAct=EBI-374969, EBI-747776; CC O75419; Q9HAW4: CLSPN; NbExp=5; IntAct=EBI-374969, EBI-1369377; CC O75419; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-374969, EBI-742054; CC O75419; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-374969, EBI-747500; CC O75419; O00629: KPNA4; NbExp=2; IntAct=EBI-374969, EBI-396343; CC O75419; P49736: MCM2; NbExp=2; IntAct=EBI-374969, EBI-374819; CC O75419; P61018: RAB4B; NbExp=3; IntAct=EBI-374969, EBI-10218066; CC O75419; P15927: RPA2; NbExp=4; IntAct=EBI-374969, EBI-621404; CC O75419; Q92547: TOPBP1; NbExp=6; IntAct=EBI-374969, EBI-308302; CC O75419; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-374969, EBI-527853; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:35585232}. Chromosome CC {ECO:0000305|PubMed:35585232}. Note=Associates with chromatin. CC {ECO:0000305|PubMed:35585232}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O75419-1; Sequence=Displayed; CC Name=2; CC IsoId=O75419-2; Sequence=VSP_043129; CC Name=3; CC IsoId=O75419-3; Sequence=VSP_045411; CC -!- TISSUE SPECIFICITY: Widely expressed, highest levels are found in adult CC testis and thymus and in fetal liver. CC -!- DEVELOPMENTAL STAGE: Transcript peaks at G1-S transition, but total CC protein remains constant throughout the cell cycle. Expressed in CC multiple tissues during embryogenesis, including neural crest-derived CC structures. CC -!- DISEASE: Meier-Gorlin syndrome 7 (MGORS7) [MIM:617063]: A form of CC Meier-Gorlin syndrome, a syndrome characterized by bilateral microtia, CC aplasia/hypoplasia of the patellae, and severe intrauterine and CC postnatal growth retardation with short stature and poor weight gain. CC Additional clinical findings include anomalies of cranial sutures, CC microcephaly, apparently low-set and simple ears, microstomia, full CC lips, highly arched or cleft palate, micrognathia, genitourinary tract CC anomalies, and various skeletal anomalies. While almost all cases have CC primordial dwarfism with substantial prenatal and postnatal growth CC retardation, not all cases have microcephaly, and microtia and CC absent/hypoplastic patella are absent in some. Despite the presence of CC microcephaly, intellect is usually normal. MGORS7 inheritance is CC autosomal recessive. {ECO:0000269|PubMed:27374770}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the CDC45 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF062495; AAC67521.1; -; mRNA. DR EMBL; AF053074; AAC27289.1; -; mRNA. DR EMBL; AJ223728; CAA11530.1; -; mRNA. DR EMBL; AF081535; AAD08998.1; -; mRNA. DR EMBL; AY358971; AAQ89330.1; -; mRNA. DR EMBL; AK293123; BAG56675.1; -; mRNA. DR EMBL; AK293338; BAG56854.1; -; mRNA. DR EMBL; BT006792; AAP35438.1; -; mRNA. DR EMBL; AY572790; AAS66985.1; -; Genomic_DNA. DR EMBL; CT841513; CAJ86443.1; -; mRNA. DR EMBL; AC000082; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC000087; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC000088; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471176; EAX03036.1; -; Genomic_DNA. DR EMBL; BC006232; AAH06232.1; -; mRNA. DR EMBL; BC010022; AAH10022.1; -; mRNA. DR CCDS; CCDS13762.1; -. [O75419-1] DR CCDS; CCDS54499.1; -. [O75419-3] DR CCDS; CCDS54500.1; -. [O75419-2] DR RefSeq; NP_001171481.1; NM_001178010.2. [O75419-3] DR RefSeq; NP_001171482.1; NM_001178011.2. [O75419-2] DR RefSeq; NP_003495.1; NM_003504.4. [O75419-1] DR RefSeq; XP_005261342.1; XM_005261285.2. DR RefSeq; XP_011528717.1; XM_011530415.1. DR RefSeq; XP_011528720.1; XM_011530418.2. [O75419-2] DR PDB; 5DGO; X-ray; 2.10 A; A=1-566. DR PDB; 6XTX; EM; 3.29 A; E=1-566. DR PDB; 6XTY; EM; 6.77 A; E=1-566. DR PDB; 7PFO; EM; 3.20 A; C=1-566. DR PDB; 7PLO; EM; 2.80 A; C=1-566. DR PDBsum; 5DGO; -. DR PDBsum; 6XTX; -. DR PDBsum; 6XTY; -. DR PDBsum; 7PFO; -. DR PDBsum; 7PLO; -. DR AlphaFoldDB; O75419; -. DR EMDB; EMD-10619; -. DR EMDB; EMD-10621; -. DR EMDB; EMD-13375; -. DR EMDB; EMD-13494; -. DR SMR; O75419; -. DR BioGRID; 113915; 130. DR ComplexPortal; CPX-4526; CMG helicase complex. DR DIP; DIP-31725N; -. DR IntAct; O75419; 79. DR MINT; O75419; -. DR STRING; 9606.ENSP00000405726; -. DR BindingDB; O75419; -. DR ChEMBL; CHEMBL3040; -. DR GlyGen; O75419; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75419; -. DR MetOSite; O75419; -. DR PhosphoSitePlus; O75419; -. DR BioMuta; CDC45; -. DR jPOST; O75419; -. DR MassIVE; O75419; -. DR PaxDb; 9606-ENSP00000405726; -. DR PeptideAtlas; O75419; -. DR ProteomicsDB; 19667; -. DR ProteomicsDB; 49990; -. [O75419-1] DR ProteomicsDB; 49991; -. [O75419-2] DR Pumba; O75419; -. DR Antibodypedia; 262; 368 antibodies from 36 providers. DR DNASU; 8318; -. DR Ensembl; ENST00000263201.7; ENSP00000263201.2; ENSG00000093009.11. [O75419-1] DR Ensembl; ENST00000404724.7; ENSP00000384978.3; ENSG00000093009.11. [O75419-2] DR Ensembl; ENST00000437685.6; ENSP00000405726.2; ENSG00000093009.11. [O75419-3] DR GeneID; 8318; -. DR KEGG; hsa:8318; -. DR MANE-Select; ENST00000263201.7; ENSP00000263201.2; NM_003504.5; NP_003495.1. DR UCSC; uc002zpr.5; human. [O75419-1] DR AGR; HGNC:1739; -. DR CTD; 8318; -. DR DisGeNET; 8318; -. DR GeneCards; CDC45; -. DR HGNC; HGNC:1739; CDC45. DR HPA; ENSG00000093009; Tissue enhanced (bone marrow, lymphoid tissue, testis). DR MalaCards; CDC45; -. DR MIM; 603465; gene. DR MIM; 617063; phenotype. DR neXtProt; NX_O75419; -. DR OpenTargets; ENSG00000093009; -. DR Orphanet; 2554; Ear-patella-short stature syndrome. DR PharmGKB; PA371; -. DR VEuPathDB; HostDB:ENSG00000093009; -. DR eggNOG; KOG2475; Eukaryota. DR GeneTree; ENSGT00390000009662; -. DR HOGENOM; CLU_005871_4_0_1; -. DR InParanoid; O75419; -. DR OMA; MYLPRQL; -. DR OrthoDB; 1407079at2759; -. DR PhylomeDB; O75419; -. DR TreeFam; TF101062; -. DR PathwayCommons; O75419; -. DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress. DR Reactome; R-HSA-176974; Unwinding of DNA. DR Reactome; R-HSA-68962; Activation of the pre-replicative complex. DR Reactome; R-HSA-69205; G1/S-Specific Transcription. DR SignaLink; O75419; -. DR SIGNOR; O75419; -. DR BioGRID-ORCS; 8318; 844 hits in 1176 CRISPR screens. DR ChiTaRS; CDC45; human. DR GeneWiki; CDC45-related_protein; -. DR GenomeRNAi; 8318; -. DR Pharos; O75419; Tbio. DR PRO; PR:O75419; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; O75419; protein. DR Bgee; ENSG00000093009; Expressed in oocyte and 106 other cell types or tissues. DR ExpressionAtlas; O75419; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0036064; C:ciliary basal body; IDA:GO_Central. DR GO; GO:0071162; C:CMG complex; IPI:ComplexPortal. DR GO; GO:0031261; C:DNA replication preinitiation complex; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000076; P:DNA replication checkpoint signaling; TAS:ProtInc. DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal. DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central. DR GO; GO:1902977; P:mitotic DNA replication preinitiation complex assembly; IBA:GO_Central. DR InterPro; IPR003874; CDC45. DR PANTHER; PTHR10507; CDC45-RELATED PROTEIN; 1. DR PANTHER; PTHR10507:SF0; CELL DIVISION CONTROL PROTEIN 45 HOMOLOG; 1. DR Pfam; PF02724; CDC45; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Chromosome; KW Disease variant; DNA replication; Dwarfism; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome. FT CHAIN 1..566 FT /note="Cell division control protein 45 homolog" FT /id="PRO_0000192815" FT REGION 136..163 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 147..163 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 130 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 144 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 68..113 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043129" FT VAR_SEQ 180 FT /note="R -> RSGSGSEPVAAALEKSSRLFAGPMSDRTAPRSP (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045411" FT VARIANT 68 FT /note="Q -> R (in MGORS7; decreased protein level; FT dbSNP:rs879255633)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080963" FT VARIANT 76 FT /note="N -> H (in MGORS7; decreased protein level; FT dbSNP:rs879255632)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080964" FT VARIANT 81 FT /note="V -> I (in dbSNP:rs13447203)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_019286" FT VARIANT 155 FT /note="E -> G (in MGORS7; uncertain significance; FT associated in cis with T-321; dbSNP:rs9606030)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080965" FT VARIANT 157 FT /note="R -> C (in MGORS7; decreased protein level; FT dbSNP:rs540217942)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080966" FT VARIANT 226 FT /note="D -> G (in MGORS7; decreased protein level; FT dbSNP:rs754080445)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080967" FT VARIANT 264 FT /note="S -> Y (in MGORS7; uncertain significance; FT dbSNP:rs151279621)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080968" FT VARIANT 298 FT /note="A -> V (in MGORS7; decreased protein level; FT dbSNP:rs146559223)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080969" FT VARIANT 321 FT /note="P -> T (in MGORS7; uncertain significance; FT associated in cis with G-155)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080970" FT VARIANT 356 FT /note="M -> R (in dbSNP:rs17209274)" FT /id="VAR_053026" FT VARIANT 376 FT /note="V -> M (in dbSNP:rs13447263)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_019287" FT VARIANT 424..566 FT /note="Missing (in MGORS7; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080971" FT VARIANT 463 FT /note="P -> L (in MGORS7; likely pathogenic; FT dbSNP:rs751663397)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080972" FT VARIANT 496 FT /note="P -> L (in MGORS7; uncertain significance; FT dbSNP:rs1376596361)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080973" FT VARIANT 554 FT /note="R -> W (in MGORS7; uncertain significance; FT dbSNP:rs778665661)" FT /evidence="ECO:0000269|PubMed:27374770" FT /id="VAR_080974" FT CONFLICT 100 FT /note="T -> S (in Ref. 5; AAQ89330)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="I -> V (in Ref. 3; CAA11530)" FT /evidence="ECO:0000305" FT CONFLICT 346 FT /note="E -> Q (in Ref. 1; AAC67521)" FT /evidence="ECO:0000305" FT CONFLICT 509 FT /note="I -> F (in Ref. 6; BAG56854)" FT /evidence="ECO:0000305" FT HELIX 6..10 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 11..14 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 17..26 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 27..42 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 46..54 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 55..65 FT /evidence="ECO:0007829|PDB:5DGO" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 70..78 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 83..87 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 106..110 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 113..117 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 130..133 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 165..189 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 198..208 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 214..229 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 235..255 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 269..277 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 281..283 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 286..292 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 294..299 FT /evidence="ECO:0007829|PDB:5DGO" FT TURN 300..303 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 305..318 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 322..326 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 329..331 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 334..350 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 356..366 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 369..372 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 373..384 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 393..403 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 410..435 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 443..449 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 457..459 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 463..480 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 486..488 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 491..498 FT /evidence="ECO:0007829|PDB:5DGO" FT TURN 499..502 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 503..509 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 522..531 FT /evidence="ECO:0007829|PDB:5DGO" FT TURN 532..534 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 541..543 FT /evidence="ECO:0007829|PDB:5DGO" FT STRAND 546..550 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 551..553 FT /evidence="ECO:0007829|PDB:5DGO" FT HELIX 554..565 FT /evidence="ECO:0007829|PDB:5DGO" SQ SEQUENCE 566 AA; 65569 MW; AE1BE2C8C8E5F867 CRC64; MFVSDFRKEF YEVVQSQRVL LFVASDVDAL CACKILQALF QCDHVQYTLV PVSGWQELET AFLEHKEQFH YFILINCGAN VDLLDILQPD EDTIFFVCDT HRPVNVVNVY NDTQIKLLIK QDDDLEVPAY EDIFRDEEED EEHSGNDSDG SEPSEKRTRL EEEIVEQTMR RRQRREWEAR RRDILFDYEQ YEYHGTSSAM VMFELAWMLS KDLNDMLWWA IVGLTDQWVQ DKITQMKYVT DVGVLQRHVS RHNHRNEDEE NTLSVDCTRI SFEYDLRLVL YQHWSLHDSL CNTSYTAARF KLWSVHGQKR LQEFLADMGL PLKQVKQKFQ AMDISLKENL REMIEESANK FGMKDMRVQT FSIHFGFKHK FLASDVVFAT MSLMESPEKD GSGTDHFIQA LDSLSRSNLD KLYHGLELAK KQLRATQQTI ASCLCTNLVI SQGPFLYCSL MEGTPDVMLF SRPASLSLLS KHLLKSFVCS TKNRRCKLLP LVMAAPLSME HGTVTVVGIP PETDSSDRKN FFGRAFEKAA ESTSSRMLHN HFDLSVIELK AEDRSKFLDA LISLLS //