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 27-MAR-2024, entry version 213. 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). RN [30] RP INTERACTION WITH FBXO43. RX PubMed=34595750; DOI=10.1111/cge.14069; RA Wu H., Zhang X., Shen Q., Liu Y., Gao Y., Wang G., Lv M., Hua R., Xu Y., RA Zhou P., Wei Z., Tao F., He X., Cao Y., Liu M.; RT "A homozygous loss-of-function mutation in FBXO43 causes human non- RT obstructive azoospermia."; RL Clin. Genet. 101:55-64(2022). 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. Interacts with FBXO43; the interaction is direct. CC {ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744, CC ECO:0000269|PubMed:34595750, 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; 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; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-396137, EBI-11519926; 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 PDB; 8PKP; EM; 3.20 A; U/V=1-597. DR PDB; 8TAR; EM; 4.00 A; U/V=1-597. DR PDB; 8TAU; EM; 3.50 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 PDBsum; 8PKP; -. DR PDBsum; 8TAR; -. DR PDBsum; 8TAU; -. DR AlphaFoldDB; Q9UJX2; -. DR EMDB; EMD-10516; -. DR EMDB; EMD-10518; -. DR EMDB; EMD-10536; -. DR EMDB; EMD-13931; -. DR EMDB; EMD-17751; -. DR EMDB; EMD-2924; -. DR EMDB; EMD-2925; -. DR EMDB; EMD-3385; -. DR EMDB; EMD-3386; -. DR EMDB; EMD-3387; -. DR EMDB; EMD-3388; -. DR EMDB; EMD-3389; -. DR EMDB; EMD-3390; -. DR EMDB; EMD-4037; -. DR EMDB; EMD-41140; -. DR EMDB; EMD-41142; -. DR EMDB; EMD-4465; -. DR EMDB; EMD-4466; -. DR EMDB; EMD-4467; -. DR SMR; Q9UJX2; -. DR BioGRID; 114242; 262. DR ComplexPortal; CPX-1860; Anaphase-promoting core complex. DR CORUM; Q9UJX2; -. DR DIP; DIP-32959N; -. DR ELM; Q9UJX2; -. DR IntAct; Q9UJX2; 179. DR MINT; Q9UJX2; -. DR STRING; 9606.ENSP00000378350; -. DR GlyGen; Q9UJX2; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9UJX2; -. DR PhosphoSitePlus; Q9UJX2; -. DR SwissPalm; Q9UJX2; -. DR BioMuta; CDC23; -. DR DMDM; 254763423; -. DR EPD; Q9UJX2; -. DR jPOST; Q9UJX2; -. DR MassIVE; Q9UJX2; -. DR MaxQB; Q9UJX2; -. DR PaxDb; 9606-ENSP00000378350; -. DR PeptideAtlas; Q9UJX2; -. DR ProteomicsDB; 84679; -. [Q9UJX2-1] DR ProteomicsDB; 84680; -. [Q9UJX2-2] DR ProteomicsDB; 84681; -. [Q9UJX2-3] DR Pumba; Q9UJX2; -. DR Antibodypedia; 14882; 357 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 AGR; HGNC:1724; -. 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; PQYLSAW; -. DR OrthoDB; 3131281at2759; -. 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; 817 hits in 1180 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 202 other cell types or tissues. DR ExpressionAtlas; Q9UJX2; baseline and differential. DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB. 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; TAS:ProtInc. DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; 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; NAS:ComplexPortal. DR GO; GO:0007346; P:regulation of mitotic cell cycle; NAS: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; Tetratricopeptide repeat domain; 2. DR InterPro; IPR007192; APC8. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR12558; CELL DIVISION CYCLE 16,23,27; 1. DR PANTHER; PTHR12558:SF10; CELL DIVISION CYCLE PROTEIN 23 HOMOLOG; 1. DR Pfam; PF04049; ANAPC8; 1. DR Pfam; PF13414; TPR_11; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 7. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS50005; TPR; 6. DR PROSITE; PS50293; TPR_REGION; 1. DR Genevisible; Q9UJX2; HS. 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 25..27 FT /evidence="ECO:0007829|PDB:8TAU" 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 //