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Database: UniProt
Entry: Q9UJX2
LinkDB: Q9UJX2
Original site: Q9UJX2 
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   17-JUN-2020, entry version 194.
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:0000244|PDB:4UI9, ECO:0000244|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; 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; 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; Q8IYA8: CCDC36; NbExp=6; IntAct=EBI-396137, EBI-8638439;
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; 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; 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; 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; Q8NC69: KCTD6; NbExp=6; IntAct=EBI-396137, EBI-2511344;
CC       Q9UJX2; O76013-2: KRT36; NbExp=3; IntAct=EBI-396137, EBI-11958506;
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; 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; 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; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-396137, EBI-2212028;
CC       Q9UJX2; P32856-2: STX2; NbExp=3; IntAct=EBI-396137, EBI-11956649;
CC       Q9UJX2; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-396137, EBI-11139477;
CC       Q9UJX2; Q15025: TNIP1; NbExp=3; IntAct=EBI-396137, EBI-357849;
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/";
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   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   SMR; Q9UJX2; -.
DR   BioGRID; 114242; 158.
DR   CORUM; Q9UJX2; -.
DR   DIP; DIP-32959N; -.
DR   ELM; Q9UJX2; -.
DR   IntAct; Q9UJX2; 156.
DR   MINT; Q9UJX2; -.
DR   STRING; 9606.ENSP00000378350; -.
DR   iPTMnet; Q9UJX2; -.
DR   PhosphoSitePlus; Q9UJX2; -.
DR   BioMuta; CDC23; -.
DR   DMDM; 254763423; -.
DR   EPD; Q9UJX2; -.
DR   jPOST; Q9UJX2; -.
DR   MassIVE; 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; 276 antibodies.
DR   DNASU; 8697; -.
DR   Ensembl; ENST00000394884; ENSP00000378348; ENSG00000094880. [Q9UJX2-2]
DR   Ensembl; ENST00000394886; ENSP00000378350; ENSG00000094880. [Q9UJX2-1]
DR   GeneID; 8697; -.
DR   KEGG; hsa:8697; -.
DR   UCSC; uc003lcl.3; human. [Q9UJX2-1]
DR   CTD; 8697; -.
DR   DisGeNET; 8697; -.
DR   EuPathDB; HostDB:ENSG00000094880.10; -.
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   eggNOG; KOG1155; Eukaryota.
DR   eggNOG; ENOG410XPS3; LUCA.
DR   GeneTree; ENSGT00950000182950; -.
DR   HOGENOM; CLU_018320_3_0_1; -.
DR   InParanoid; Q9UJX2; -.
DR   KO; K03355; -.
DR   OMA; EYDRCAA; -.
DR   OrthoDB; 761109at2759; -.
DR   PhylomeDB; Q9UJX2; -.
DR   TreeFam; TF101055; -.
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-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; Q9UJX2; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 8697; 730 hits in 789 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 female gonad and 221 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:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005622; C:intracellular; IDA:LIFEdb.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   DisProt; DP01240; -.
DR   Gene3D; 1.25.40.10; -; 2.
DR   InterPro; IPR007192; APC8.
DR   InterPro; IPR013026; TPR-contain_dom.
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; Polymorphism; Reference proteome;
KW   Repeat; TPR repeat; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|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:0000244|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:0000244|PubMed:19608861"
FT   MOD_RES         562
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000269|PubMed:14657031"
FT   MOD_RES         565
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   MOD_RES         578
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         582
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332"
FT   MOD_RES         588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         593
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         596
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   CROSSLNK        147
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|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:0000244|PDB:6Q6G"
FT   HELIX           49..61
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            67..69
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           78..81
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           84..95
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           99..105
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           112..133
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          137..139
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   TURN            140..142
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          143..145
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           149..163
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           170..181
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           185..198
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           203..210
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           216..221
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           229..240
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           244..257
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           259..261
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           263..276
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           279..292
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           300..308
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            309..311
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           313..326
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          328..330
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           331..343
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           347..360
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          361..363
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           365..377
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           381..394
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           399..411
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           415..428
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           434..445
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           449..461
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           469..479
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           484..499
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           513..516
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           519..522
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           527..532
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            533..538
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           543..553
FT                   /evidence="ECO:0000244|PDB:6Q6G"
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
//
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