CDC20_HUMAN
ID CDC20_HUMAN Reviewed; 499 AA.
AC Q12834; B2R6Z6; D3DPJ1; Q5JUY4; Q9BW56; Q9UQI9;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Cell division cycle protein 20 homolog;
DE AltName: Full=p55CDC;
GN Name=CDC20;
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].
RX PubMed=7513050; DOI=10.1128/mcb.14.5.3350-3363.1994;
RA Weinstein J., Jacobsen F.W., Hsu-Chen J., Wu T., Baum L.G.;
RT "A novel mammalian protein, p55CDC, present in dividing cells is associated
RT with protein kinase activity and has homology to the Saccharomyces
RT cerevisiae cell division cycle proteins Cdc20 and Cdc4.";
RL Mol. Cell. Biol. 14:3350-3363(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH MAD2L1 AND
RP APC/C.
RC TISSUE=Liver, and Spleen;
RX PubMed=9811605; DOI=10.1016/s0960-9822(07)00510-6;
RA Kramer E.R., Gieffers C., Hoelzl G., Hengstschlaeger M., Peters J.-M.;
RT "Activation of the human anaphase-promoting complex by proteins of the
RT CDC20/Fizzy family.";
RL Curr. Biol. 8:1207-1210(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-402 AND GLN-479.
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Colon adenocarcinoma, Lymph, Muscle, Ovary, and Skin;
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 [9]
RP FUNCTION, AND INTERACTION WITH APC/C.
RX PubMed=9734353; DOI=10.1016/s1097-2765(00)80126-4;
RA Fang G., Yu H., Kirschner M.W.;
RT "Direct binding of CDC20 protein family members activates the anaphase-
RT promoting complex in mitosis and G1.";
RL Mol. Cell 2:163-171(1998).
RN [10]
RP FUNCTION, AND INTERACTION WITH MAD2L1 AND APC/C.
RX PubMed=9637688; DOI=10.1101/gad.12.12.1871;
RA Fang G., Yu H., Kirschner M.W.;
RT "The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary
RT complex with the anaphase-promoting complex to control anaphase
RT initiation.";
RL Genes Dev. 12:1871-1883(1998).
RN [11]
RP PHOSPHORYLATION.
RX PubMed=10459014; DOI=10.1083/jcb.146.4.791;
RA Kotani S., Tanaka H., Yasuda H., Todokoro K.;
RT "Regulation of APC activity by phosphorylation and regulatory factors.";
RL J. Cell Biol. 146:791-800(1999).
RN [12]
RP INTERACTION WITH MAD2L2.
RX PubMed=11459826; DOI=10.1101/gad.898701;
RA Chen J., Fang G.;
RT "MAD2B is an inhibitor of the anaphase-promoting complex.";
RL Genes Dev. 15:1765-1770(2001).
RN [13]
RP PHOSPHORYLATION AT THR-70 AND THR-106.
RX PubMed=14657031; DOI=10.1093/emboj/cdg627;
RA Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,
RA Peters J.-M.;
RT "Mitotic regulation of the human anaphase-promoting complex by
RT phosphorylation.";
RL EMBO J. 22:6598-6609(2003).
RN [14]
RP PHOSPHORYLATION AT SER-41; SER-72; SER-92; SER-153; THR-157 AND SER-161,
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BUB1B AND MAD2L1, AND
RP MUTAGENESIS OF SER-41; SER-72; SER-92; SER-153; THR-157 AND SER-161.
RX PubMed=15525512; DOI=10.1016/j.molcel.2004.09.031;
RA Tang Z., Shu H., Oncel D., Chen S., Yu H.;
RT "Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C
RT inhibition by the spindle checkpoint.";
RL Mol. Cell 16:387-397(2004).
RN [15]
RP INTERACTION WITH NINL.
RX PubMed=17403670; DOI=10.1074/jbc.m701350200;
RA Wang Y., Zhan Q.;
RT "Cell cycle-dependent expression of centrosomal ninein-like protein in
RT human cells is regulated by the anaphase-promoting complex.";
RL J. Biol. Chem. 282:17712-17719(2007).
RN [16]
RP UBIQUITINATION, AND DEUBIQUITINATION BY USP44.
RX PubMed=17443180; DOI=10.1038/nature05694;
RA Stegmeier F., Rape M., Draviam V.M., Nalepa G., Sowa M.E., Ang X.L.,
RA McDonald E.R. III, Li M.Z., Hannon G.J., Sorger P.K., Kirschner M.W.,
RA Harper J.W., Elledge S.J.;
RT "Anaphase initiation is regulated by antagonistic ubiquitination and
RT deubiquitination activities.";
RL Nature 446:876-881(2007).
RN [17]
RP INTERACTION WITH HSF1.
RX PubMed=18794143; DOI=10.1158/0008-5472.can-08-0129;
RA Lee Y.J., Kim E.H., Lee J.S., Jeoung D., Bae S., Kwon S.H., Lee Y.S.;
RT "HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is essential
RT for mitotic progression.";
RL Cancer Res. 68:7550-7560(2008).
RN [18]
RP UBIQUITINATION, INTERACTION WITH BUB1B, AND DEGRADATION BY THE PROTEASOME.
RX PubMed=18997788; DOI=10.1038/ncb1799;
RA Nilsson J., Yekezare M., Minshull J., Pines J.;
RT "The APC/C maintains the spindle assembly checkpoint by targeting Cdc20 for
RT destruction.";
RL Nat. Cell Biol. 10:1411-1420(2008).
RN [19]
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 [20]
RP UBIQUITINATION, INTERACTION WITH MAD2L1 AND BUB1B, DEGRADATION BY THE
RP PROTEASOME, AND MUTAGENESIS OF ARG-132.
RX PubMed=19098431; DOI=10.4161/cc.8.1.7606;
RA Ge S., Skaar J.R., Pagano M.;
RT "APC/C- and Mad2-mediated degradation of Cdc20 during spindle checkpoint
RT activation.";
RL Cell Cycle 8:167-171(2009).
RN [21]
RP INTERACTION WITH CDK5RAP2.
RX PubMed=19282672; DOI=10.4161/cc.8.8.8205;
RA Zhang X., Liu D., Lv S., Wang H., Zhong X., Liu B., Wang B., Liao J.,
RA Li J., Pfeifer G.P., Xu X.;
RT "CDK5RAP2 is required for spindle checkpoint function.";
RL Cell Cycle 8:1206-1216(2009).
RN [22]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH NEK2.
RX PubMed=20034488; DOI=10.1016/j.yexmp.2009.12.004;
RA Liu Q., Hirohashi Y., Du X., Greene M.I., Wang Q.;
RT "Nek2 targets the mitotic checkpoint proteins Mad2 and Cdc20: a mechanism
RT for aneuploidy in cancer.";
RL Exp. Mol. Pathol. 88:225-233(2010).
RN [23]
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 [24]
RP UBIQUITINATION AT LYS-485 AND LYS-490, AND MUTAGENESIS OF LYS-485 AND
RP LYS-490.
RX PubMed=21926987; DOI=10.1038/ncb2347;
RA Mansfeld J., Collin P., Collins M.O., Choudhary J.S., Pines J.;
RT "APC15 drives the turnover of MCC-CDC20 to make the spindle assembly
RT checkpoint responsive to kinetochore attachment.";
RL Nat. Cell Biol. 13:1234-1243(2011).
RN [25]
RP ACETYLATION AT LYS-66, DEACETYLATION AT LYS-66 BY SIRT2, AND INTERACTION
RP WITH SIRT2.
RX PubMed=22014574; DOI=10.1016/j.ccr.2011.09.004;
RA Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C.,
RA Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I.,
RA Gius D., Deng C.X.;
RT "SIRT2 maintains genome integrity and suppresses tumorigenesis through
RT regulating APC/C activity.";
RL Cancer Cell 20:487-499(2011).
RN [26]
RP DEPHOSPHORYLATION.
RX PubMed=22692537; DOI=10.1038/ncomms1886;
RA Visconti R., Palazzo L., Della Monica R., Grieco D.;
RT "Fcp1-dependent dephosphorylation is required for M-phase-promoting factor
RT inactivation at mitosis exit.";
RL Nat. Commun. 3:894-894(2012).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND THR-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [28]
RP INTERACTION WITH CCNF.
RX PubMed=27653696; DOI=10.1016/j.celrep.2016.08.058;
RA Choudhury R., Bonacci T., Arceci A., Lahiri D., Mills C.A., Kernan J.L.,
RA Branigan T.B., DeCaprio J.A., Burke D.J., Emanuele M.J.;
RT "APC/C and SCF(cyclin F) Constitute a Reciprocal Feedback Circuit
RT Controlling S-Phase Entry.";
RL Cell Rep. 16:3359-3372(2016).
RN [29]
RP INTERACTION WITH MAD2L1.
RX PubMed=29162720; DOI=10.1074/jbc.ra117.000555;
RA Ji W., Luo Y., Ahmad E., Liu S.T.;
RT "Direct interactions of mitotic arrest deficient 1 (MAD1) domains with each
RT other and MAD2 conformers are required for mitotic checkpoint signaling.";
RL J. Biol. Chem. 293:484-496(2018).
CC -!- FUNCTION: Required for full ubiquitin ligase activity of the anaphase
CC promoting complex/cyclosome (APC/C) and may confer substrate
CC specificity upon the complex. Is regulated by MAD2L1: in metaphase the
CC MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the
CC CDC20-APC/C binary complex is active in degrading substrates. The
CC CDC20-APC/C complex positively regulates the formation of synaptic
CC vesicle clustering at active zone to the presynaptic membrane in
CC postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces
CC presynaptic differentiation. {ECO:0000269|PubMed:9637688,
CC ECO:0000269|PubMed:9734353, ECO:0000269|PubMed:9811605}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of a complex with CDC20, CDC27, SPATC1 and TUBG1 (By
CC similarity). Interacts with NEUROD2 (By similarity). Interacts with
CC dimeric MAD2L1 in its closed conformation form (PubMed:9811605,
CC PubMed:9637688, PubMed:15525512, PubMed:19098431, PubMed:29162720).
CC Interacts with BUB1B (PubMed:15525512, PubMed:18997788,
CC PubMed:19098431). The phosphorylated form interacts with APC/C
CC (PubMed:9811605, PubMed:9734353, PubMed:9637688). Interacts with NINL
CC (PubMed:17403670). May interact with MAD2L2 (PubMed:11459826).
CC Interacts with CDK5RAP2 (PubMed:19282672). Interacts with SIRT2
CC (PubMed:22014574). Interacts with isoform 1 of NEK2 (PubMed:20034488).
CC Interacts with HSF1 (via phosphorylated form); this interaction occurs
CC in mitosis in a MAD2L1-dependent manner and prevents PLK1-stimulated
CC degradation of HSF1 by blocking the recruitment of the SCF(BTRC)
CC ubiquitin ligase complex (PubMed:18794143). Interacts (via the N-
CC terminal substrate-binding domain) with FBXO5 (By similarity).
CC Interacts with CCNF (PubMed:27653696). {ECO:0000250|UniProtKB:Q9JJ66,
CC ECO:0000269|PubMed:11459826, ECO:0000269|PubMed:15525512,
CC ECO:0000269|PubMed:17403670, ECO:0000269|PubMed:18794143,
CC ECO:0000269|PubMed:18997788, ECO:0000269|PubMed:19098431,
CC ECO:0000269|PubMed:19282672, ECO:0000269|PubMed:20034488,
CC ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:27653696,
CC ECO:0000269|PubMed:29162720, ECO:0000269|PubMed:9637688,
CC ECO:0000269|PubMed:9734353, ECO:0000269|PubMed:9811605}.
CC -!- INTERACTION:
CC Q12834; Q9UJX5: ANAPC4; NbExp=9; IntAct=EBI-367462, EBI-2554854;
CC Q12834; O60566: BUB1B; NbExp=33; IntAct=EBI-367462, EBI-1001438;
CC Q12834; P30260: CDC27; NbExp=12; IntAct=EBI-367462, EBI-994813;
CC Q12834; Q13257: MAD2L1; NbExp=34; IntAct=EBI-367462, EBI-78203;
CC Q12834; Q9UI95: MAD2L2; NbExp=2; IntAct=EBI-367462, EBI-77889;
CC Q12834; Q9NS23-2: RASSF1; NbExp=2; IntAct=EBI-367462, EBI-438698;
CC Q12834; Q8IXJ6-2: SIRT2; NbExp=2; IntAct=EBI-367462, EBI-5240785;
CC Q12834; O88566: Axin2; Xeno; NbExp=2; IntAct=EBI-367462, EBI-7690990;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:20034488}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:20034488}.
CC -!- DEVELOPMENTAL STAGE: Synthesis is initiated at G1/S, protein level
CC peaks in M phase and protein is abruptly degraded at M/G1 transition.
CC -!- PTM: Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation
CC enhances the interaction of CDC20 with CDC27, leading to activation of
CC anaphase promoting complex/cyclosome (APC/C).
CC {ECO:0000269|PubMed:22014574}.
CC -!- PTM: Phosphorylated during mitosis, probably by maturation promoting
CC factor (MPF). Phosphorylated by BUB1 at Ser-41; Ser-72; Ser-92; Ser-
CC 153; Thr-157 and Ser-161. Phosphorylated by NEK2.
CC {ECO:0000269|PubMed:10459014, ECO:0000269|PubMed:14657031,
CC ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:20034488}.
CC -!- PTM: Dephosphorylated by CTDP1.
CC -!- PTM: Ubiquitinated and degraded by the proteasome during spindle
CC assembly checkpoint. Deubiquitinated by USP44, leading to stabilize the
CC MAD2L1-CDC20-APC/C ternary complex, thereby preventing premature
CC activation of the APC/C. Ubiquitinated at Lys-490 during prometaphase.
CC Ubiquitination at Lys-485 and Lys-490 has no effect on its ability to
CC bind the APC/C complex. {ECO:0000269|PubMed:17443180,
CC ECO:0000269|PubMed:18997788, ECO:0000269|PubMed:19098431,
CC ECO:0000269|PubMed:21926987}.
CC -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CDC20ID40003ch1p34.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc20/";
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DR EMBL; U05340; AAA19017.1; -; mRNA.
DR EMBL; AF099644; AAD16405.1; -; mRNA.
DR EMBL; AK312780; BAG35643.1; -; mRNA.
DR EMBL; BT007388; AAP36052.1; -; mRNA.
DR EMBL; DQ473545; ABE96834.1; -; Genomic_DNA.
DR EMBL; AL139289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07101.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07102.1; -; Genomic_DNA.
DR EMBL; BC000624; AAH00624.1; -; mRNA.
DR EMBL; BC001088; AAH01088.1; -; mRNA.
DR EMBL; BC006272; AAH06272.1; -; mRNA.
DR EMBL; BC009425; AAH09425.1; -; mRNA.
DR EMBL; BC009426; AAH09426.1; -; mRNA.
DR EMBL; BC010044; AAH10044.1; -; mRNA.
DR EMBL; BC012803; AAH12803.1; -; mRNA.
DR EMBL; BC012827; AAH12827.1; -; mRNA.
DR EMBL; BC013303; AAH13303.1; -; mRNA.
DR EMBL; BC015998; AAH15998.1; -; mRNA.
DR EMBL; BC024257; AAH24257.1; -; mRNA.
DR EMBL; BC031294; AAH31294.1; -; mRNA.
DR EMBL; BC110321; AAI10322.1; -; mRNA.
DR CCDS; CCDS484.1; -.
DR PIR; A56021; A56021.
DR RefSeq; NP_001246.2; NM_001255.2.
DR PDB; 4GGA; X-ray; 2.04 A; A=81-499.
DR PDB; 4GGC; X-ray; 1.35 A; A=161-477.
DR PDB; 4GGD; X-ray; 2.44 A; A/B=71-499.
DR PDB; 4N14; X-ray; 2.10 A; A=165-477.
DR PDB; 5G04; EM; 4.00 A; R=1-499.
DR PDB; 5KHR; EM; 6.10 A; R=1-499.
DR PDB; 5KHU; EM; 4.80 A; R/S=1-499.
DR PDB; 5LCW; EM; 4.00 A; Q=126-499, R=1-499.
DR PDB; 6F0X; EM; 4.60 A; Q=1-499.
DR PDB; 6Q6G; EM; 3.20 A; R=1-499.
DR PDB; 6Q6H; EM; 3.20 A; R=1-499.
DR PDBsum; 4GGA; -.
DR PDBsum; 4GGC; -.
DR PDBsum; 4GGD; -.
DR PDBsum; 4N14; -.
DR PDBsum; 5G04; -.
DR PDBsum; 5KHR; -.
DR PDBsum; 5KHU; -.
DR PDBsum; 5LCW; -.
DR PDBsum; 6F0X; -.
DR PDBsum; 6Q6G; -.
DR PDBsum; 6Q6H; -.
DR AlphaFoldDB; Q12834; -.
DR SMR; Q12834; -.
DR BioGRID; 107427; 212.
DR ComplexPortal; CPX-3946; Mitotic Checkpoint Complex.
DR ComplexPortal; CPX-6087; Anaphase-Promoting complex, CDC20 variant.
DR CORUM; Q12834; -.
DR DIP; DIP-29655N; -.
DR ELM; Q12834; -.
DR IntAct; Q12834; 72.
DR MINT; Q12834; -.
DR STRING; 9606.ENSP00000361540; -.
DR BindingDB; Q12834; -.
DR ChEMBL; CHEMBL4523283; -.
DR TCDB; 8.A.92.1.14; the g-protein AlphaBetaGama complex (gpc) family.
DR iPTMnet; Q12834; -.
DR PhosphoSitePlus; Q12834; -.
DR SwissPalm; Q12834; -.
DR BioMuta; CDC20; -.
DR DMDM; 37537762; -.
DR EPD; Q12834; -.
DR jPOST; Q12834; -.
DR MassIVE; Q12834; -.
DR MaxQB; Q12834; -.
DR PaxDb; Q12834; -.
DR PeptideAtlas; Q12834; -.
DR PRIDE; Q12834; -.
DR ProteomicsDB; 58976; -.
DR Antibodypedia; 3864; 716 antibodies from 38 providers.
DR DNASU; 991; -.
DR Ensembl; ENST00000310955.11; ENSP00000308450.5; ENSG00000117399.14.
DR Ensembl; ENST00000372462.1; ENSP00000361540.1; ENSG00000117399.14.
DR GeneID; 991; -.
DR KEGG; hsa:991; -.
DR MANE-Select; ENST00000310955.11; ENSP00000308450.5; NM_001255.3; NP_001246.2.
DR UCSC; uc001cix.4; human.
DR CTD; 991; -.
DR DisGeNET; 991; -.
DR GeneCards; CDC20; -.
DR HGNC; HGNC:1723; CDC20.
DR HPA; ENSG00000117399; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 603618; gene.
DR neXtProt; NX_Q12834; -.
DR OpenTargets; ENSG00000117399; -.
DR PharmGKB; PA26257; -.
DR VEuPathDB; HostDB:ENSG00000117399; -.
DR eggNOG; KOG0305; Eukaryota.
DR GeneTree; ENSGT00950000183104; -.
DR HOGENOM; CLU_014831_6_1_1; -.
DR InParanoid; Q12834; -.
DR OMA; NGHEDRV; -.
DR OrthoDB; 1220675at2759; -.
DR PhylomeDB; Q12834; -.
DR TreeFam; TF101065; -.
DR PathwayCommons; Q12834; -.
DR Reactome; R-HSA-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-HSA-176417; Phosphorylation of Emi1.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q12834; -.
DR SIGNOR; Q12834; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 991; 808 hits in 1107 CRISPR screens.
DR ChiTaRS; CDC20; human.
DR GeneWiki; CDC20; -.
DR GenomeRNAi; 991; -.
DR Pharos; Q12834; Tbio.
DR PRO; PR:Q12834; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q12834; protein.
DR Bgee; ENSG00000117399; Expressed in oocyte and 137 other tissues.
DR Genevisible; Q12834; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0033597; C:mitotic checkpoint complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; TAS:ProtInc.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:ComplexPortal.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR DisProt; DP01118; -.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR033010; Cdc20/Fizzy.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19918; PTHR19918; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Differentiation; Isopeptide bond; Mitosis; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..499
FT /note="Cell division cycle protein 20 homolog"
FT /id="PRO_0000050900"
FT REPEAT 182..221
FT /note="WD 1"
FT REPEAT 224..263
FT /note="WD 2"
FT REPEAT 266..303
FT /note="WD 3"
FT REPEAT 307..346
FT /note="WD 4"
FT REPEAT 353..395
FT /note="WD 5"
FT REPEAT 397..438
FT /note="WD 6"
FT REPEAT 441..480
FT /note="WD 7"
FT REGION 17..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15525512,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22014574"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15525512"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15525512"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15525512"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15525512"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15525512"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:21926987"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:21926987"
FT VARIANT 402
FT /note="V -> M (in dbSNP:rs45443196)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_030368"
FT VARIANT 479
FT /note="R -> Q (in dbSNP:rs45461499)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_030369"
FT MUTAGEN 41
FT /note="S->A: Loss of BUB1-mediated phosphorylation and
FT inhibition and partially defective spindle-assembly
FT checkpoint; when associated with A-72; A-92; A-153; A-157
FT and A-161."
FT /evidence="ECO:0000269|PubMed:15525512"
FT MUTAGEN 72
FT /note="S->A: Loss of BUB1-mediated phosphorylation and
FT inhibition and partially defective spindle-assembly
FT checkpoint; when associated with A-41; A-92; A-153; A-157
FT and A-161."
FT /evidence="ECO:0000269|PubMed:15525512"
FT MUTAGEN 92
FT /note="S->A: Loss of BUB1-mediated phosphorylation and
FT inhibition and partially defective spindle-assembly
FT checkpoint; when associated with A-41; A-72; A-153; A-157
FT and A-161."
FT /evidence="ECO:0000269|PubMed:15525512"
FT MUTAGEN 132
FT /note="R->A: Loss of interaction with MAD2L1."
FT /evidence="ECO:0000269|PubMed:19098431"
FT MUTAGEN 153
FT /note="S->A: Loss of BUB1-mediated phosphorylation and
FT inhibition and partially defective spindle-assembly
FT checkpoint; when associated with A-42; A-72; A-92; A-157
FT and A-161."
FT /evidence="ECO:0000269|PubMed:15525512"
FT MUTAGEN 157
FT /note="T->A: Loss of BUB1-mediated phosphorylation and
FT inhibition and partially defective spindle-assembly
FT checkpoint; when associated with A-42; A-72; A-92; A-153
FT and A-161."
FT /evidence="ECO:0000269|PubMed:15525512"
FT MUTAGEN 161
FT /note="S->A: Loss of BUB1-mediated phosphorylation and
FT inhibition and partially defective spindle-assembly
FT checkpoint; when associated with A-72; A-92; A-153; A-157
FT and A-161."
FT /evidence="ECO:0000269|PubMed:15525512"
FT MUTAGEN 485
FT /note="K->R: Does not affect its ability to bind the APC/C
FT complex; when associated with R-490."
FT /evidence="ECO:0000269|PubMed:21926987"
FT MUTAGEN 490
FT /note="K->R: Does not affect its ability to bind the APC/C
FT complex; when associated with R-485."
FT /evidence="ECO:0000269|PubMed:21926987"
FT CONFLICT 101
FT /note="P -> S (in Ref. 1; AAA19017)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="A -> V (in Ref. 8; AAH00624)"
FT /evidence="ECO:0000305"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:6Q6G"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4GGC"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:4GGC"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6Q6H"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:4GGC"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:4GGC"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:4GGC"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:4GGC"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:4GGC"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:4GGC"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:4GGC"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:4GGC"
SQ 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
