CDC45_HUMAN
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 03-AUG-2022, entry version 189.
DE RecName: Full=Cell division control protein 45 homolog;
DE AltName: Full=PORC-PI-1;
GN Name=CDC45; Synonyms=CDC45L, CDC45L2; 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 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.
CC -!- SUBUNIT: Associated with ORC2. Interacts with HELB (PubMed:25933514).
CC Component of the CMG helicase complex, composed of the MCM2-7 complex,
CC the GINS complex and CDC45 (By similarity).
CC {ECO:0000250|UniProtKB:Q9YHZ6, ECO:0000269|PubMed:25933514}.
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=4; IntAct=EBI-374969, EBI-1369377;
CC O75419; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-374969, EBI-742054;
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: Cytoplasm. Nucleus.
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 -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc45l/";
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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 SMR; O75419; -.
DR BioGRID; 113915; 118.
DR ComplexPortal; CPX-4526; CMG helicase complex.
DR DIP; DIP-31725N; -.
DR IntAct; O75419; 36.
DR MINT; O75419; -.
DR STRING; 9606.ENSP00000405726; -.
DR BindingDB; O75419; -.
DR ChEMBL; CHEMBL3040; -.
DR iPTMnet; O75419; -.
DR MetOSite; O75419; -.
DR PhosphoSitePlus; O75419; -.
DR BioMuta; CDC45; -.
DR EPD; O75419; -.
DR jPOST; O75419; -.
DR MassIVE; O75419; -.
DR MaxQB; O75419; -.
DR PeptideAtlas; O75419; -.
DR PRIDE; O75419; -.
DR ProteomicsDB; 19667; -.
DR ProteomicsDB; 49990; -. [O75419-1]
DR ProteomicsDB; 49991; -. [O75419-2]
DR Antibodypedia; 262; 370 antibodies from 37 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 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; PWNLANV; -.
DR OrthoDB; 1309031at2759; -.
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 BioGRID-ORCS; 8318; 811 hits in 1097 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 104 other tissues.
DR ExpressionAtlas; O75419; baseline and differential.
DR Genevisible; O75419; HS.
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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; PTHR10507; 1.
DR Pfam; PF02724; CDC45; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; Disease variant;
KW DNA replication; Dwarfism; Nucleus; Phosphoprotein; 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; unknown pathological
FT significance; associated in cis with T-321;
FT 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; unknown pathological
FT significance; 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; unknown pathological
FT significance; 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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27374770"
FT /id="VAR_080971"
FT VARIANT 463
FT /note="P -> L (in MGORS7; unknown pathological
FT significance; dbSNP:rs751663397)"
FT /evidence="ECO:0000269|PubMed:27374770"
FT /id="VAR_080972"
FT VARIANT 496
FT /note="P -> L (in MGORS7; unknown pathological
FT significance; dbSNP:rs1376596361)"
FT /evidence="ECO:0000269|PubMed:27374770"
FT /id="VAR_080973"
FT VARIANT 554
FT /note="R -> W (in MGORS7; unknown pathological
FT significance; 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