位置:首页 > 蛋白库 > CDC45_HUMAN
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/";
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   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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024