CDC23_HUMAN
ID CDC23_HUMAN Reviewed; 597 AA.
AC Q9UJX2; A8K6E5; B4E3A2; B7WP05; D3DQB7; O75433; Q53FN2; Q9BS73;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Cell division cycle protein 23 homolog;
DE AltName: Full=Anaphase-promoting complex subunit 8;
DE Short=APC8;
DE AltName: Full=Cyclosome subunit 8;
GN Name=CDC23; Synonyms=ANAPC8;
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).
RA Oyamatsu T., Kotani S., Todokoro K.;
RT "Human CDC23 gene.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-78.
RG NIEHS SNPs program;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 5-597 (ISOFORM 1).
RC TISSUE=Brain, Duodenum, and Pancreas;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-597 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9790767; DOI=10.1006/geno.1998.5473;
RA Zhao N., Lai F., Fernald A.A., Eisenbart J.D., Espinosa R., Wang P.W.,
RA Le Beau M.M.;
RT "Human CDC23: cDNA cloning, mapping to 5q31, genomic structure, and
RT evaluation as a candidate tumor suppressor gene in myeloid leukemias.";
RL Genomics 53:184-190(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-597 (ISOFORM 1), AND SUBUNIT.
RX PubMed=9469815; DOI=10.1126/science.279.5354.1219;
RA Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.;
RT "Identification of a cullin homology region in a subunit of the anaphase-
RT promoting complex.";
RL Science 279:1219-1222(1998).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-597 (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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PHOSPHORYLATION AT TYR-273; THR-562 AND THR-565.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP FUNCTION OF THE APC/C.
RX PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
RA Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
RT "Mechanism of ubiquitin-chain formation by the human anaphase-promoting
RT complex.";
RL Cell 133:653-665(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562; THR-582; SER-588;
RP SER-593 AND THR-596, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; THR-582; SER-588 AND
RP THR-596, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-467, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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 [20]
RP TPR REPEATS.
RX PubMed=21307936; DOI=10.1038/nature09756;
RA Schreiber A., Stengel F., Zhang Z., Enchev R.I., Kong E.H., Morris E.P.,
RA Robinson C.V., da Fonseca P.C., Barford D.;
RT "Structural basis for the subunit assembly of the anaphase-promoting
RT complex.";
RL Nature 470:227-232(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; SER-588; SER-593 AND
RP THR-596, AND 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE APC/C.
RX PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
RA Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
RA Engel A., Peters J.-M., Stark H.;
RT "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
RT cryo-electron microscopy model of vertebrate APC/C.";
RL Mol. Cell 20:867-879(2005).
RN [28]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, AND SUBUNIT.
RX PubMed=25043029; DOI=10.1038/nature13543;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Molecular architecture and mechanism of the anaphase-promoting complex.";
RL Nature 513:388-393(2014).
RN [29] {ECO:0007744|PDB:4UI9, ECO:0007744|PDB:5A31}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 7-597 OF APC/C,
RP SUBUNIT, AND MUTAGENESIS OF ASN-339 AND GLU-374.
RX PubMed=26083744; DOI=10.1038/nature14471;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Atomic structure of the APC/C and its mechanism of protein
RT ubiquitination.";
RL Nature 522:450-454(2015).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle. The
CC APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation of
CC 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
CC {ECO:0000269|PubMed:18485873}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC ANAPC16 that assemble into a complex of at least 19 chains with a
CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC and FBXO5. {ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744,
CC ECO:0000269|PubMed:9469815}.
CC -!- INTERACTION:
CC Q9UJX2; A8K3Z6: ANAPC13; NbExp=3; IntAct=EBI-396137, EBI-10322710;
CC Q9UJX2; Q9BS18: ANAPC13; NbExp=7; IntAct=EBI-396137, EBI-2555953;
CC Q9UJX2; X5D778: ANKRD11; NbExp=3; IntAct=EBI-396137, EBI-17183751;
CC Q9UJX2; O14791: APOL1; NbExp=3; IntAct=EBI-396137, EBI-1221934;
CC Q9UJX2; Q8WXE1: ATRIP; NbExp=3; IntAct=EBI-396137, EBI-747353;
CC Q9UJX2; P54253: ATXN1; NbExp=6; IntAct=EBI-396137, EBI-930964;
CC Q9UJX2; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-396137, EBI-702390;
CC Q9UJX2; P46379-2: BAG6; NbExp=3; IntAct=EBI-396137, EBI-10988864;
CC Q9UJX2; Q9H6U6: BCAS3; NbExp=3; IntAct=EBI-396137, EBI-6083685;
CC Q9UJX2; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-396137, EBI-742722;
CC Q9UJX2; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-396137, EBI-11519926;
CC Q9UJX2; Q13895: BYSL; NbExp=5; IntAct=EBI-396137, EBI-358049;
CC Q9UJX2; P55212: CASP6; NbExp=3; IntAct=EBI-396137, EBI-718729;
CC Q9UJX2; Q8NA61: CBY2; NbExp=3; IntAct=EBI-396137, EBI-741724;
CC Q9UJX2; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-396137, EBI-11977221;
CC Q9UJX2; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-396137, EBI-1104933;
CC Q9UJX2; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-396137, EBI-744115;
CC Q9UJX2; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-396137, EBI-12261896;
CC Q9UJX2; P38432: COIL; NbExp=3; IntAct=EBI-396137, EBI-945751;
CC Q9UJX2; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-396137, EBI-739773;
CC Q9UJX2; Q53ET0: CRTC2; NbExp=3; IntAct=EBI-396137, EBI-1181987;
CC Q9UJX2; Q6BCY4: CYB5R2; NbExp=3; IntAct=EBI-396137, EBI-744761;
CC Q9UJX2; O15075-2: DCLK1; NbExp=3; IntAct=EBI-396137, EBI-12324841;
CC Q9UJX2; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-396137, EBI-11988027;
CC Q9UJX2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-396137, EBI-10976677;
CC Q9UJX2; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-396137, EBI-12593112;
CC Q9UJX2; Q9GZV4: EIF5A2; NbExp=3; IntAct=EBI-396137, EBI-748028;
CC Q9UJX2; Q9NYK6-3: EURL; NbExp=3; IntAct=EBI-396137, EBI-13371226;
CC Q9UJX2; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-396137, EBI-10175124;
CC Q9UJX2; A4D1I3: FLJ34048; NbExp=3; IntAct=EBI-396137, EBI-10173415;
CC Q9UJX2; O15353: FOXN1; NbExp=3; IntAct=EBI-396137, EBI-11319000;
CC Q9UJX2; O95073: FSBP; NbExp=3; IntAct=EBI-396137, EBI-1059030;
CC Q9UJX2; P14136: GFAP; NbExp=3; IntAct=EBI-396137, EBI-744302;
CC Q9UJX2; Q9H8Y8: GORASP2; NbExp=9; IntAct=EBI-396137, EBI-739467;
CC Q9UJX2; Q8N3Z3: GTPBP8; NbExp=3; IntAct=EBI-396137, EBI-6912536;
CC Q9UJX2; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-396137, EBI-10329202;
CC Q9UJX2; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-396137, EBI-8638439;
CC Q9UJX2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-396137, EBI-6509505;
CC Q9UJX2; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-396137, EBI-769401;
CC Q9UJX2; Q15735: INPP5J; NbExp=3; IntAct=EBI-396137, EBI-10236940;
CC Q9UJX2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-396137, EBI-1055254;
CC Q9UJX2; Q8NC69: KCTD6; NbExp=6; IntAct=EBI-396137, EBI-2511344;
CC Q9UJX2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-396137, EBI-10975473;
CC Q9UJX2; O14901: KLF11; NbExp=3; IntAct=EBI-396137, EBI-948266;
CC Q9UJX2; O76013-2: KRT36; NbExp=3; IntAct=EBI-396137, EBI-11958506;
CC Q9UJX2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-396137, EBI-21591415;
CC Q9UJX2; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-396137, EBI-12039345;
CC Q9UJX2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-396137, EBI-1216080;
CC Q9UJX2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-396137, EBI-741037;
CC Q9UJX2; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-396137, EBI-716006;
CC Q9UJX2; Q15742: NAB2; NbExp=3; IntAct=EBI-396137, EBI-8641936;
CC Q9UJX2; Q96F24: NRBF2; NbExp=3; IntAct=EBI-396137, EBI-2362014;
CC Q9UJX2; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-396137, EBI-741048;
CC Q9UJX2; Q96CV9: OPTN; NbExp=8; IntAct=EBI-396137, EBI-748974;
CC Q9UJX2; Q16877: PFKFB4; NbExp=3; IntAct=EBI-396137, EBI-764534;
CC Q9UJX2; O14832: PHYH; NbExp=3; IntAct=EBI-396137, EBI-721853;
CC Q9UJX2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-396137, EBI-10232538;
CC Q9UJX2; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-396137, EBI-10171633;
CC Q9UJX2; P78424: POU6F2; NbExp=3; IntAct=EBI-396137, EBI-12029004;
CC Q9UJX2; Q2NL68: PROSER3; NbExp=3; IntAct=EBI-396137, EBI-11336487;
CC Q9UJX2; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-396137, EBI-1567797;
CC Q9UJX2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-396137, EBI-5280197;
CC Q9UJX2; P60891: PRPS1; NbExp=3; IntAct=EBI-396137, EBI-749195;
CC Q9UJX2; P63000: RAC1; NbExp=3; IntAct=EBI-396137, EBI-413628;
CC Q9UJX2; Q8NDT2-2: RBM15B; NbExp=3; IntAct=EBI-396137, EBI-10269922;
CC Q9UJX2; P10745: RBP3; NbExp=3; IntAct=EBI-396137, EBI-12806054;
CC Q9UJX2; Q93062: RBPMS; NbExp=4; IntAct=EBI-396137, EBI-740322;
CC Q9UJX2; Q9UHA3: RSL24D1; NbExp=3; IntAct=EBI-396137, EBI-749321;
CC Q9UJX2; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-396137, EBI-11984663;
CC Q9UJX2; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-396137, EBI-747107;
CC Q9UJX2; Q9HAB3: SLC52A2; NbExp=3; IntAct=EBI-396137, EBI-10309896;
CC Q9UJX2; Q53HV7: SMUG1; NbExp=3; IntAct=EBI-396137, EBI-749970;
CC Q9UJX2; O60504: SORBS3; NbExp=3; IntAct=EBI-396137, EBI-741237;
CC Q9UJX2; P35711: SOX5; NbExp=3; IntAct=EBI-396137, EBI-3505701;
CC Q9UJX2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-396137, EBI-11959123;
CC Q9UJX2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-396137, EBI-5235340;
CC Q9UJX2; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-396137, EBI-2212028;
CC Q9UJX2; P32856-2: STX2; NbExp=3; IntAct=EBI-396137, EBI-11956649;
CC Q9UJX2; Q13148: TARDBP; NbExp=3; IntAct=EBI-396137, EBI-372899;
CC Q9UJX2; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-396137, EBI-11139477;
CC Q9UJX2; Q15025: TNIP1; NbExp=3; IntAct=EBI-396137, EBI-357849;
CC Q9UJX2; O14656-2: TOR1A; NbExp=3; IntAct=EBI-396137, EBI-25847109;
CC Q9UJX2; P14373: TRIM27; NbExp=4; IntAct=EBI-396137, EBI-719493;
CC Q9UJX2; Q9Y3Q8: TSC22D4; NbExp=4; IntAct=EBI-396137, EBI-739485;
CC Q9UJX2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-396137, EBI-11975223;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UJX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJX2-2; Sequence=VSP_008429, VSP_008430;
CC Name=3;
CC IsoId=Q9UJX2-3; Sequence=VSP_037678;
CC -!- PTM: Phosphorylated. Phosphorylation on Thr-562 occurs specifically
CC during mitosis. {ECO:0000269|PubMed:14657031}.
CC -!- SIMILARITY: Belongs to the APC8/CDC23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC70920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH05258.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH10944.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH17713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS99353.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA75628.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD96970.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAF84299.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc23/";
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DR EMBL; AB011472; BAA75628.1; ALT_INIT; mRNA.
DR EMBL; AK291610; BAF84299.1; ALT_INIT; mRNA.
DR EMBL; AK304635; BAG65414.1; -; mRNA.
DR EMBL; AY603103; AAS99353.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK223250; BAD96970.1; ALT_INIT; mRNA.
DR EMBL; AC106752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62155.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62154.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62156.1; -; Genomic_DNA.
DR EMBL; BC005258; AAH05258.1; ALT_INIT; mRNA.
DR EMBL; BC010944; AAH10944.1; ALT_INIT; mRNA.
DR EMBL; BC017713; AAH17713.1; ALT_INIT; mRNA.
DR EMBL; AF053977; AAC70920.1; ALT_INIT; mRNA.
DR EMBL; AF191341; AAF05755.1; -; mRNA.
DR EMBL; BT009810; AAP88812.1; -; mRNA.
DR CCDS; CCDS4200.2; -. [Q9UJX2-1]
DR PIR; T51168; T51168.
DR RefSeq; NP_004652.2; NM_004661.3. [Q9UJX2-1]
DR PDB; 4UI9; EM; 3.60 A; C/P=7-597.
DR PDB; 5A31; EM; 4.30 A; C/P=1-597.
DR PDB; 5G04; EM; 4.00 A; C/P=1-597.
DR PDB; 5G05; EM; 3.40 A; C/P=1-597.
DR PDB; 5KHR; EM; 6.10 A; C/P=1-597.
DR PDB; 5KHU; EM; 4.80 A; C/P=1-597.
DR PDB; 5L9T; EM; 6.40 A; C/P=1-597.
DR PDB; 5L9U; EM; 6.40 A; C/P=1-597.
DR PDB; 5LCW; EM; 4.00 A; C/P=1-597.
DR PDB; 6Q6G; EM; 3.20 A; U/V=1-597.
DR PDB; 6Q6H; EM; 3.20 A; U/V=1-597.
DR PDB; 6TLJ; EM; 3.80 A; C/P=1-597.
DR PDB; 6TM5; EM; 3.90 A; C/P=1-597.
DR PDB; 6TNT; EM; 3.78 A; C/P=1-597.
DR PDB; 7QE7; EM; 2.90 A; U/V=1-597.
DR PDBsum; 4UI9; -.
DR PDBsum; 5A31; -.
DR PDBsum; 5G04; -.
DR PDBsum; 5G05; -.
DR PDBsum; 5KHR; -.
DR PDBsum; 5KHU; -.
DR PDBsum; 5L9T; -.
DR PDBsum; 5L9U; -.
DR PDBsum; 5LCW; -.
DR PDBsum; 6Q6G; -.
DR PDBsum; 6Q6H; -.
DR PDBsum; 6TLJ; -.
DR PDBsum; 6TM5; -.
DR PDBsum; 6TNT; -.
DR PDBsum; 7QE7; -.
DR AlphaFoldDB; Q9UJX2; -.
DR SMR; Q9UJX2; -.
DR BioGRID; 114242; 244.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR CORUM; Q9UJX2; -.
DR DIP; DIP-32959N; -.
DR ELM; Q9UJX2; -.
DR IntAct; Q9UJX2; 176.
DR MINT; Q9UJX2; -.
DR STRING; 9606.ENSP00000378350; -.
DR GlyGen; Q9UJX2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJX2; -.
DR PhosphoSitePlus; Q9UJX2; -.
DR BioMuta; CDC23; -.
DR DMDM; 254763423; -.
DR EPD; Q9UJX2; -.
DR jPOST; Q9UJX2; -.
DR MassIVE; Q9UJX2; -.
DR MaxQB; Q9UJX2; -.
DR PaxDb; Q9UJX2; -.
DR PeptideAtlas; Q9UJX2; -.
DR PRIDE; Q9UJX2; -.
DR ProteomicsDB; 84679; -. [Q9UJX2-1]
DR ProteomicsDB; 84680; -. [Q9UJX2-2]
DR ProteomicsDB; 84681; -. [Q9UJX2-3]
DR Antibodypedia; 14882; 309 antibodies from 40 providers.
DR DNASU; 8697; -.
DR Ensembl; ENST00000394884.7; ENSP00000378348.3; ENSG00000094880.11. [Q9UJX2-2]
DR Ensembl; ENST00000394886.7; ENSP00000378350.2; ENSG00000094880.11. [Q9UJX2-1]
DR GeneID; 8697; -.
DR KEGG; hsa:8697; -.
DR MANE-Select; ENST00000394886.7; ENSP00000378350.2; NM_004661.4; NP_004652.2.
DR UCSC; uc003lcl.3; human. [Q9UJX2-1]
DR CTD; 8697; -.
DR DisGeNET; 8697; -.
DR GeneCards; CDC23; -.
DR HGNC; HGNC:1724; CDC23.
DR HPA; ENSG00000094880; Low tissue specificity.
DR MIM; 603462; gene.
DR neXtProt; NX_Q9UJX2; -.
DR OpenTargets; ENSG00000094880; -.
DR PharmGKB; PA26258; -.
DR VEuPathDB; HostDB:ENSG00000094880; -.
DR eggNOG; KOG1155; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_018320_3_0_1; -.
DR InParanoid; Q9UJX2; -.
DR OMA; PKYLAAW; -.
DR OrthoDB; 761109at2759; -.
DR PhylomeDB; Q9UJX2; -.
DR TreeFam; TF101055; -.
DR PathwayCommons; Q9UJX2; -.
DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
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-176412; Phosphorylation of the APC/C.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UJX2; -.
DR SIGNOR; Q9UJX2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8697; 783 hits in 1092 CRISPR screens.
DR ChiTaRS; CDC23; human.
DR GeneWiki; CDC23; -.
DR GenomeRNAi; 8697; -.
DR Pharos; Q9UJX2; Tbio.
DR PRO; PR:Q9UJX2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UJX2; protein.
DR Bgee; ENSG00000094880; Expressed in adrenal tissue and 200 other tissues.
DR ExpressionAtlas; Q9UJX2; baseline and differential.
DR Genevisible; Q9UJX2; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IDA:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007096; P:regulation of exit from mitosis; TAS:ProtInc.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR DisProt; DP01240; -.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR007192; APC8.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF04049; ANAPC8; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Isopeptide bond; Mitosis; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..597
FT /note="Cell division cycle protein 23 homolog"
FT /id="PRO_0000106270"
FT REPEAT 27..63
FT /note="TPR 1"
FT REPEAT 73..112
FT /note="TPR 2"
FT REPEAT 114..144
FT /note="TPR 3"
FT REPEAT 169..200
FT /note="TPR 4"
FT REPEAT 229..259
FT /note="TPR 5"
FT REPEAT 263..293
FT /note="TPR 6"
FT REPEAT 297..327
FT /note="TPR 7"
FT REPEAT 331..361
FT /note="TPR 8"
FT REPEAT 366..395
FT /note="TPR 9"
FT REPEAT 400..432
FT /note="TPR 10"
FT REPEAT 433..466
FT /note="TPR 11"
FT REPEAT 468..500
FT /note="TPR 12"
FT REPEAT 504..540
FT /note="TPR 13"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 273
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 467
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 565
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 582
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037678"
FT VAR_SEQ 125..151
FT /note="SGEKKKDDETVDSLGPLEKGQVKNEAL -> VRAILKCHSAFSETSIFRTNG
FT KVKSFK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008429"
FT VAR_SEQ 152..597
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008430"
FT VARIANT 9
FT /note="P -> L (in dbSNP:rs2231471)"
FT /id="VAR_024675"
FT VARIANT 78
FT /note="E -> Q (in dbSNP:rs17228304)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019232"
FT MUTAGEN 339
FT /note="N->A: Inhibits APC/FZR1 E3 ubiquitin-protein ligase
FT complex activity; when associated with A-374."
FT /evidence="ECO:0000269|PubMed:26083744"
FT MUTAGEN 374
FT /note="E->A: Inhibits APC/FZR1 E3 ubiquitin-protein ligase
FT complex activity; when associated with A-339."
FT /evidence="ECO:0000269|PubMed:26083744"
FT CONFLICT 83
FT /note="D -> E (in Ref. 4; BAD96970)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="F -> S (in Ref. 4; BAD96970)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="D -> G (in Ref. 2; BAG65414)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="S -> F (in Ref. 9; AAF05755)"
FT /evidence="ECO:0000305"
FT HELIX 29..45
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5G05"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 381..394
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 399..411
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 433..444
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 449..461
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 484..499
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 509..520
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 543..558
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:7QE7"
SQ SEQUENCE 597 AA; 68834 MW; 358F2B8745DB9D32 CRC64;
MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF
SLPALPLAEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD RAAHFLHGCN SKKAYFLYMY
SRYLSGEKKK DDETVDSLGP LEKGQVKNEA LRELRVELSK KHQARELDGF GLYLYGVVLR
KLDLVKEAID VFVEATHVLP LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE
LQLIEEALQK YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM
DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA ALYFQRALKL
NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR AWYGLGQTYE ILKMPFYCLY
YYRRAHQLRP NDSRMLVALG ECYEKLNQLV EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL
TESEQAAQCY IKYIQDIYSC GEIVEHLEES TAFRYLAQYY FKCKLWDEAS TCAQKCCAFN
DTREEGKALL RQILQLRNQG ETPTTEVPAP FFLPASLSAN NTPTRRVSPL NLSSVTP
