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Cell division cycle protein 20 homolog (p55CDC)

 CDC20_HUMAN             Reviewed;         499 AA.
Q12834; B2R6Z6; D3DPJ1; Q5JUY4; Q9BW56; Q9UQI9;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
03-OCT-2003, sequence version 2.
22-NOV-2017, entry version 177.
RecName: Full=Cell division cycle protein 20 homolog;
AltName: Full=p55CDC;
Name=CDC20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7513050; DOI=10.1128/MCB.14.5.3350;
Weinstein J., Jacobsen F.W., Hsu-Chen J., Wu T., Baum L.G.;
"A novel mammalian protein, p55CDC, present in dividing cells is
associated with protein kinase activity and has homology to the
Saccharomyces cerevisiae cell division cycle proteins Cdc20 and
Cdc4.";
Mol. Cell. Biol. 14:3350-3363(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH MAD2L1 AND
APC/C.
TISSUE=Liver, and Spleen;
PubMed=9811605; DOI=10.1016/S0960-9822(07)00510-6;
Kramer E.R., Gieffers C., Hoelzl G., Hengstschlaeger M., Peters J.-M.;
"Activation of the human anaphase-promoting complex by proteins of the
CDC20/Fizzy family.";
Curr. Biol. 8:1207-1210(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-402 AND GLN-479.
NIEHS SNPs program;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, Colon adenocarcinoma, Lymph, Muscle, Ovary, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, AND INTERACTION WITH APC/C.
PubMed=9734353; DOI=10.1016/S1097-2765(00)80126-4;
Fang G., Yu H., Kirschner M.W.;
"Direct binding of CDC20 protein family members activates the
anaphase-promoting complex in mitosis and G1.";
Mol. Cell 2:163-171(1998).
[10]
FUNCTION, AND INTERACTION WITH MAD2L1 AND APC/C.
PubMed=9637688; DOI=10.1101/gad.12.12.1871;
Fang G., Yu H., Kirschner M.W.;
"The checkpoint protein MAD2 and the mitotic regulator CDC20 form a
ternary complex with the anaphase-promoting complex to control
anaphase initiation.";
Genes Dev. 12:1871-1883(1998).
[11]
PHOSPHORYLATION.
PubMed=10459014; DOI=10.1083/jcb.146.4.791;
Kotani S., Tanaka H., Yasuda H., Todokoro K.;
"Regulation of APC activity by phosphorylation and regulatory
factors.";
J. Cell Biol. 146:791-800(1999).
[12]
INTERACTION WITH MAD2L2.
PubMed=11459826; DOI=10.1101/gad.898701;
Chen J., Fang G.;
"MAD2B is an inhibitor of the anaphase-promoting complex.";
Genes Dev. 15:1765-1770(2001).
[13]
PHOSPHORYLATION AT THR-70 AND THR-106.
PubMed=14657031; DOI=10.1093/emboj/cdg627;
Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,
Peters J.-M.;
"Mitotic regulation of the human anaphase-promoting complex by
phosphorylation.";
EMBO J. 22:6598-6609(2003).
[14]
PHOSPHORYLATION AT SER-41; SER-72; SER-92; SER-153; THR-157 AND
SER-161, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BUB1B
AND MAD2L1, AND MUTAGENESIS OF SER-41; SER-72; SER-92; SER-153;
THR-157 AND SER-161.
PubMed=15525512; DOI=10.1016/j.molcel.2004.09.031;
Tang Z., Shu H., Oncel D., Chen S., Yu H.;
"Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for
APC/C inhibition by the spindle checkpoint.";
Mol. Cell 16:387-397(2004).
[15]
INTERACTION WITH NINL.
PubMed=17403670; DOI=10.1074/jbc.M701350200;
Wang Y., Zhan Q.;
"Cell cycle-dependent expression of centrosomal ninein-like protein in
human cells is regulated by the anaphase-promoting complex.";
J. Biol. Chem. 282:17712-17719(2007).
[16]
UBIQUITINATION, AND DEUBIQUITINATION BY USP44.
PubMed=17443180; DOI=10.1038/nature05694;
Stegmeier F., Rape M., Draviam V.M., Nalepa G., Sowa M.E., Ang X.L.,
McDonald E.R. III, Li M.Z., Hannon G.J., Sorger P.K., Kirschner M.W.,
Harper J.W., Elledge S.J.;
"Anaphase initiation is regulated by antagonistic ubiquitination and
deubiquitination activities.";
Nature 446:876-881(2007).
[17]
INTERACTION WITH HSF1.
PubMed=18794143; DOI=10.1158/0008-5472.CAN-08-0129;
Lee Y.J., Kim E.H., Lee J.S., Jeoung D., Bae S., Kwon S.H., Lee Y.S.;
"HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is
essential for mitotic progression.";
Cancer Res. 68:7550-7560(2008).
[18]
UBIQUITINATION, INTERACTION WITH BUB1B, AND DEGRADATION BY THE
PROTEASOME.
PubMed=18997788; DOI=10.1038/ncb1799;
Nilsson J., Yekezare M., Minshull J., Pines J.;
"The APC/C maintains the spindle assembly checkpoint by targeting
Cdc20 for destruction.";
Nat. Cell Biol. 10:1411-1420(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
UBIQUITINATION, INTERACTION WITH MAD2L1 AND BUB1B, DEGRADATION BY THE
PROTEASOME, AND MUTAGENESIS OF ARG-132.
PubMed=19098431; DOI=10.4161/cc.8.1.7606;
Ge S., Skaar J.R., Pagano M.;
"APC/C- and Mad2-mediated degradation of Cdc20 during spindle
checkpoint activation.";
Cell Cycle 8:167-171(2009).
[21]
INTERACTION WITH CDK5RAP2.
PubMed=19282672; DOI=10.4161/cc.8.8.8205;
Zhang X., Liu D., Lv S., Wang H., Zhong X., Liu B., Wang B., Liao J.,
Li J., Pfeifer G.P., Xu X.;
"CDK5RAP2 is required for spindle checkpoint function.";
Cell Cycle 8:1206-1216(2009).
[22]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH NEK2.
PubMed=20034488; DOI=10.1016/j.yexmp.2009.12.004;
Liu Q., Hirohashi Y., Du X., Greene M.I., Wang Q.;
"Nek2 targets the mitotic checkpoint proteins Mad2 and Cdc20: a
mechanism for aneuploidy in cancer.";
Exp. Mol. Pathol. 88:225-233(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
UBIQUITINATION AT LYS-485 AND LYS-490, AND MUTAGENESIS OF LYS-485 AND
LYS-490.
PubMed=21926987; DOI=10.1038/ncb2347;
Mansfeld J., Collin P., Collins M.O., Choudhary J.S., Pines J.;
"APC15 drives the turnover of MCC-CDC20 to make the spindle assembly
checkpoint responsive to kinetochore attachment.";
Nat. Cell Biol. 13:1234-1243(2011).
[25]
ACETYLATION AT LYS-66, DEACETYLATION AT LYS-66 BY SIRT2, AND
INTERACTION WITH SIRT2.
PubMed=22014574; DOI=10.1016/j.ccr.2011.09.004;
Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X.,
Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H.,
Cha Y.I., Gius D., Deng C.X.;
"SIRT2 maintains genome integrity and suppresses tumorigenesis through
regulating APC/C activity.";
Cancer Cell 20:487-499(2011).
[26]
DEPHOSPHORYLATION.
PubMed=22692537; DOI=10.1038/ncomms1886;
Visconti R., Palazzo L., Della Monica R., Grieco D.;
"Fcp1-dependent dephosphorylation is required for M-phase-promoting
factor inactivation at mitosis exit.";
Nat. Commun. 3:894-894(2012).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND THR-70, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Required for full ubiquitin ligase activity of the
anaphase promoting complex/cyclosome (APC/C) and may confer
substrate specificity upon the complex. Is regulated by MAD2L1: in
metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and
in anaphase the CDC20-APC/C binary complex is active in degrading
substrates. The CDC20-APC/C complex positively regulates the
formation of synaptic vesicle clustering at active zone to the
presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced
degradation of NEUROD2 induces presynaptic differentiation.
{ECO:0000269|PubMed:9637688, ECO:0000269|PubMed:9734353,
ECO:0000269|PubMed:9811605}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Found in a complex with CDC20, CDC27, SPATC1 and TUBG1.
Interacts with NEUROD2 and SPATC1 (By similarity). Interacts with
MAD2L1 and BUB1B. The phosphorylated form interacts with APC/C.
Interacts with NINL. May interact with MAD2L2. Interacts with
CDK5RAP2 and SIRT2. Interacts with isoform 1 of NEK2. Interacts
with HSF1 (via phosphorylated form); this interaction occurs in
mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated
degradation of HSF1 by blocking the recruitment of the SCF(BTRC)
ubiquitin ligase complex (PubMed:18794143). {ECO:0000250,
ECO:0000269|PubMed:11459826, ECO:0000269|PubMed:15525512,
ECO:0000269|PubMed:17403670, ECO:0000269|PubMed:18794143,
ECO:0000269|PubMed:18997788, ECO:0000269|PubMed:19098431,
ECO:0000269|PubMed:19282672, ECO:0000269|PubMed:20034488,
ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:9637688,
ECO:0000269|PubMed:9734353, ECO:0000269|PubMed:9811605}.
-!- INTERACTION:
Q9UJX5:ANAPC4; NbExp=9; IntAct=EBI-367462, EBI-2554854;
O88566:Axin2 (xeno); NbExp=2; IntAct=EBI-367462, EBI-7690990;
O60566:BUB1B; NbExp=30; IntAct=EBI-367462, EBI-1001438;
P30260:CDC27; NbExp=12; IntAct=EBI-367462, EBI-994813;
Q13257:MAD2L1; NbExp=33; IntAct=EBI-367462, EBI-78203;
Q9UI95:MAD2L2; NbExp=2; IntAct=EBI-367462, EBI-77889;
Q9NS23-2:RASSF1; NbExp=2; IntAct=EBI-367462, EBI-438698;
Q8IXJ6-2:SIRT2; NbExp=2; IntAct=EBI-367462, EBI-5240785;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:20034488}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:20034488}.
-!- DEVELOPMENTAL STAGE: Synthesis is initiated at G1/S, protein level
peaks in M phase and protein is abruptly degraded at M/G1
transition.
-!- PTM: Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation
enhances the interaction of CDC20 with CDC27, leading to
activation of anaphase promoting complex/cyclosome (APC/C).
{ECO:0000269|PubMed:22014574}.
-!- PTM: Phosphorylated during mitosis, probably by maturation
promoting factor (MPF). Phosphorylated by BUB1 at Ser-41; Ser-72;
Ser-92; Ser-153; Thr-157 and Ser-161. Phosphorylated by NEK2.
{ECO:0000269|PubMed:10459014, ECO:0000269|PubMed:14657031,
ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:20034488}.
-!- PTM: Dephosphorylated by CTDP1.
-!- PTM: Ubiquitinated and degraded by the proteasome during spindle
assembly checkpoint. Deubiquitinated by USP44, leading to
stabilize the MAD2L1-CDC20-APC/C ternary complex, thereby
preventing premature activation of the APC/C. Ubiquitinated at
Lys-490 during prometaphase. Ubiquitination at Lys-485 and Lys-490
has no effect on its ability to bind the APC/C complex.
{ECO:0000269|PubMed:17443180, ECO:0000269|PubMed:18997788,
ECO:0000269|PubMed:19098431, ECO:0000269|PubMed:21926987}.
-!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDC20ID40003ch1p34.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc20/";
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EMBL; U05340; AAA19017.1; -; mRNA.
EMBL; AF099644; AAD16405.1; -; mRNA.
EMBL; AK312780; BAG35643.1; -; mRNA.
EMBL; BT007388; AAP36052.1; -; mRNA.
EMBL; DQ473545; ABE96834.1; -; Genomic_DNA.
EMBL; AL139289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07101.1; -; Genomic_DNA.
EMBL; CH471059; EAX07102.1; -; Genomic_DNA.
EMBL; BC000624; AAH00624.1; -; mRNA.
EMBL; BC001088; AAH01088.1; -; mRNA.
EMBL; BC006272; AAH06272.1; -; mRNA.
EMBL; BC009425; AAH09425.1; -; mRNA.
EMBL; BC009426; AAH09426.1; -; mRNA.
EMBL; BC010044; AAH10044.1; -; mRNA.
EMBL; BC012803; AAH12803.1; -; mRNA.
EMBL; BC012827; AAH12827.1; -; mRNA.
EMBL; BC013303; AAH13303.1; -; mRNA.
EMBL; BC015998; AAH15998.1; -; mRNA.
EMBL; BC024257; AAH24257.1; -; mRNA.
EMBL; BC031294; AAH31294.1; -; mRNA.
EMBL; BC110321; AAI10322.1; -; mRNA.
CCDS; CCDS484.1; -.
PIR; A56021; A56021.
RefSeq; NP_001246.2; NM_001255.2.
UniGene; Hs.524947; -.
PDB; 4GGA; X-ray; 2.04 A; A=81-499.
PDB; 4GGC; X-ray; 1.35 A; A=161-477.
PDB; 4GGD; X-ray; 2.44 A; A/B=71-499.
PDB; 4N14; X-ray; 2.10 A; A=165-477.
PDB; 5G04; EM; 4.00 A; R=1-499.
PDB; 5KHR; EM; 6.10 A; R=1-499.
PDB; 5KHU; EM; 4.80 A; R/S=1-499.
PDB; 5LCW; EM; 4.00 A; Q=126-499, R=1-499.
PDBsum; 4GGA; -.
PDBsum; 4GGC; -.
PDBsum; 4GGD; -.
PDBsum; 4N14; -.
PDBsum; 5G04; -.
PDBsum; 5KHR; -.
PDBsum; 5KHU; -.
PDBsum; 5LCW; -.
ProteinModelPortal; Q12834; -.
SMR; Q12834; -.
BioGrid; 107427; 173.
CORUM; Q12834; -.
DIP; DIP-29655N; -.
ELM; Q12834; -.
IntAct; Q12834; 57.
MINT; MINT-2211271; -.
STRING; 9606.ENSP00000308450; -.
iPTMnet; Q12834; -.
PhosphoSitePlus; Q12834; -.
BioMuta; CDC20; -.
DMDM; 37537762; -.
EPD; Q12834; -.
MaxQB; Q12834; -.
PaxDb; Q12834; -.
PeptideAtlas; Q12834; -.
PRIDE; Q12834; -.
DNASU; 991; -.
Ensembl; ENST00000310955; ENSP00000308450; ENSG00000117399.
Ensembl; ENST00000372462; ENSP00000361540; ENSG00000117399.
GeneID; 991; -.
KEGG; hsa:991; -.
UCSC; uc001cix.4; human.
CTD; 991; -.
DisGeNET; 991; -.
EuPathDB; HostDB:ENSG00000117399.13; -.
GeneCards; CDC20; -.
H-InvDB; HIX0034879; -.
HGNC; HGNC:1723; CDC20.
HPA; CAB004525; -.
HPA; HPA045842; -.
HPA; HPA055288; -.
MIM; 603618; gene.
neXtProt; NX_Q12834; -.
OpenTargets; ENSG00000117399; -.
PharmGKB; PA26257; -.
eggNOG; KOG0305; Eukaryota.
eggNOG; ENOG410XQ8I; LUCA.
GeneTree; ENSGT00870000136444; -.
HOGENOM; HOG000195514; -.
HOVERGEN; HBG001024; -.
InParanoid; Q12834; -.
KO; K03363; -.
OMA; WQSNILA; -.
OrthoDB; EOG091G06FJ; -.
PhylomeDB; Q12834; -.
TreeFam; TF101065; -.
Reactome; R-HSA-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
Reactome; R-HSA-176417; Phosphorylation of Emi1.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q12834; -.
SIGNOR; Q12834; -.
UniPathway; UPA00143; -.
ChiTaRS; CDC20; human.
GeneWiki; CDC20; -.
GenomeRNAi; 991; -.
PMAP-CutDB; Q12834; -.
PRO; PR:Q12834; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117399; -.
CleanEx; HS_CDC20; -.
Genevisible; Q12834; HS.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0005819; C:spindle; TAS:ProtInc.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0010997; F:anaphase-promoting complex binding; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:InterPro.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; TAS:ProtInc.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:Ensembl.
GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:Ensembl.
GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR024977; Apc4_WD40_dom.
InterPro; IPR033187; CDC20.
InterPro; IPR033010; Cdc20/Fizzy.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR19918; PTHR19918; 1.
PANTHER; PTHR19918:SF3; PTHR19918:SF3; 1.
Pfam; PF12894; ANAPC4_WD40; 1.
Pfam; PF00400; WD40; 4.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 3.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Cytoskeleton; Differentiation;
Isopeptide bond; Mitosis; Neurogenesis; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway;
WD repeat.
CHAIN 1 499 Cell division cycle protein 20 homolog.
/FTId=PRO_0000050900.
REPEAT 182 221 WD 1.
REPEAT 224 263 WD 2.
REPEAT 266 303 WD 3.
REPEAT 307 346 WD 4.
REPEAT 353 395 WD 5.
REPEAT 397 438 WD 6.
REPEAT 441 480 WD 7.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15525512}.
MOD_RES 66 66 N6-acetyllysine.
{ECO:0000269|PubMed:22014574}.
MOD_RES 70 70 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14657031}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000269|PubMed:15525512}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000269|PubMed:15525512}.
MOD_RES 106 106 Phosphothreonine.
{ECO:0000269|PubMed:14657031}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000269|PubMed:15525512}.
MOD_RES 157 157 Phosphothreonine.
{ECO:0000269|PubMed:15525512}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000269|PubMed:15525512}.
CROSSLNK 485 485 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21926987}.
CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21926987}.
VARIANT 402 402 V -> M (in dbSNP:rs45443196).
{ECO:0000269|Ref.5}.
/FTId=VAR_030368.
VARIANT 479 479 R -> Q (in dbSNP:rs45461499).
{ECO:0000269|Ref.5}.
/FTId=VAR_030369.
MUTAGEN 41 41 S->A: Loss of BUB1-mediated
phosphorylation and inhibition and
partially defective spindle-assembly
checkpoint; when associated with A-72; A-
92; A-153; A-157 and A-161.
{ECO:0000269|PubMed:15525512}.
MUTAGEN 72 72 S->A: Loss of BUB1-mediated
phosphorylation and inhibition and
partially defective spindle-assembly
checkpoint; when associated with A-41; A-
92; A-153; A-157 and A-161.
{ECO:0000269|PubMed:15525512}.
MUTAGEN 92 92 S->A: Loss of BUB1-mediated
phosphorylation and inhibition and
partially defective spindle-assembly
checkpoint; when associated with A-41; A-
72; A-153; A-157 and A-161.
{ECO:0000269|PubMed:15525512}.
MUTAGEN 132 132 R->A: Loss of interaction with MAD2L1.
{ECO:0000269|PubMed:19098431}.
MUTAGEN 153 153 S->A: Loss of BUB1-mediated
phosphorylation and inhibition and
partially defective spindle-assembly
checkpoint; when associated with A-42; A-
72; A-92; A-157 and A-161.
{ECO:0000269|PubMed:15525512}.
MUTAGEN 157 157 T->A: Loss of BUB1-mediated
phosphorylation and inhibition and
partially defective spindle-assembly
checkpoint; when associated with A-42; A-
72; A-92; A-153 and A-161.
{ECO:0000269|PubMed:15525512}.
MUTAGEN 161 161 S->A: Loss of BUB1-mediated
phosphorylation and inhibition and
partially defective spindle-assembly
checkpoint; when associated with A-72; A-
92; A-153; A-157 and A-161.
{ECO:0000269|PubMed:15525512}.
MUTAGEN 485 485 K->R: Does not affect its ability to bind
the APC/C complex; when associated with
R-490. {ECO:0000269|PubMed:21926987}.
MUTAGEN 490 490 K->R: Does not affect its ability to bind
the APC/C complex; when associated with
R-485. {ECO:0000269|PubMed:21926987}.
CONFLICT 101 101 P -> S (in Ref. 1; AAA19017).
{ECO:0000305}.
CONFLICT 117 117 A -> V (in Ref. 8; AAH00624).
{ECO:0000305}.
STRAND 173 177 {ECO:0000244|PDB:4GGC}.
STRAND 190 192 {ECO:0000244|PDB:4GGC}.
STRAND 196 202 {ECO:0000244|PDB:4GGC}.
STRAND 205 210 {ECO:0000244|PDB:4GGC}.
TURN 211 213 {ECO:0000244|PDB:4GGC}.
STRAND 216 221 {ECO:0000244|PDB:4GGC}.
STRAND 229 234 {ECO:0000244|PDB:4GGC}.
STRAND 238 245 {ECO:0000244|PDB:4GGC}.
STRAND 248 254 {ECO:0000244|PDB:4GGC}.
TURN 255 258 {ECO:0000244|PDB:4GGC}.
STRAND 259 265 {ECO:0000244|PDB:4GGC}.
STRAND 271 277 {ECO:0000244|PDB:4GGC}.
STRAND 280 285 {ECO:0000244|PDB:4GGC}.
STRAND 288 294 {ECO:0000244|PDB:4GGC}.
STRAND 297 299 {ECO:0000244|PDB:4GGC}.
STRAND 301 306 {ECO:0000244|PDB:4GGC}.
STRAND 312 317 {ECO:0000244|PDB:4GGC}.
STRAND 321 328 {ECO:0000244|PDB:4GGC}.
STRAND 333 339 {ECO:0000244|PDB:4GGC}.
STRAND 348 351 {ECO:0000244|PDB:4GGC}.
STRAND 358 363 {ECO:0000244|PDB:4GGC}.
STRAND 370 375 {ECO:0000244|PDB:4GGC}.
TURN 377 379 {ECO:0000244|PDB:4GGC}.
STRAND 381 386 {ECO:0000244|PDB:4GGC}.
TURN 387 389 {ECO:0000244|PDB:4GGC}.
STRAND 392 397 {ECO:0000244|PDB:4GGC}.
STRAND 402 408 {ECO:0000244|PDB:4GGC}.
TURN 409 412 {ECO:0000244|PDB:4GGC}.
STRAND 413 418 {ECO:0000244|PDB:4GGC}.
TURN 420 422 {ECO:0000244|PDB:4GGC}.
STRAND 425 429 {ECO:0000244|PDB:4GGC}.
TURN 430 432 {ECO:0000244|PDB:4GGC}.
STRAND 435 439 {ECO:0000244|PDB:4GGC}.
STRAND 446 451 {ECO:0000244|PDB:4GGC}.
STRAND 458 462 {ECO:0000244|PDB:4GGC}.
TURN 463 465 {ECO:0000244|PDB:4GGC}.
STRAND 466 470 {ECO:0000244|PDB:4GGC}.
SEQUENCE 499 AA; 54723 MW; FD5C967AF84089E8 CRC64;
MAQFAFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH SAGRTPGRTP
GKSSSKVQTT PSKPGGDRYI PHRSAAQMEV ASFLLSKENQ PENSQTPTKK EHQKAWALNL
NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV LYSQKATPGS SRKTCRYIPS LPDRILDAPE
IRNDYYLNLV DWSSGNVLAV ALDNSVYLWS ASSGDILQLL QMEQPGEYIS SVAWIKEGNY
LAVGTSSAEV QLWDVQQQKR LRNMTSHSAR VGSLSWNSYI LSSGSRSGHI HHHDVRVAEH
HVATLSGHSQ EVCGLRWAPD GRHLASGGND NLVNVWPSAP GEGGWVPLQT FTQHQGAVKA
VAWCPWQSNV LATGGGTSDR HIRIWNVCSG ACLSAVDAHS QVCSILWSPH YKELISGHGF
AQNQLVIWKY PTMAKVAELK GHTSRVLSLT MSPDGATVAS AAADETLRLW RCFELDPARR
REREKASAAK SSLIHQGIR


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