CDC16_HUMAN
ID CDC16_HUMAN Reviewed; 620 AA.
AC Q13042; A2A365; Q5T8C8; Q7Z651; Q96AE6; Q9Y564;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Cell division cycle protein 16 homolog;
DE AltName: Full=Anaphase-promoting complex subunit 6;
DE Short=APC6;
DE AltName: Full=CDC16 homolog;
DE Short=CDC16Hs;
DE AltName: Full=Cyclosome subunit 6;
GN Name=CDC16; Synonyms=ANAPC6;
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 2), AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=7736578; DOI=10.1016/0092-8674(95)90336-4;
RA Tugendreich S., Tomkiel J., Earnshaw W., Hieter P.;
RT "CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic spindle and
RT is essential for the metaphase to anaphase transition.";
RL Cell 81:261-268(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3).
RA Zhou P.K., Rigaud O.;
RT "The differential splicing variants of human CDC16 mRNA.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH PPP5C.
RX PubMed=9405394; DOI=10.1074/jbc.272.51.32011;
RA Ollendorff V., Donoghue D.J.;
RT "The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two
RT tetratricopeptide repeat-containing subunits of the anaphase-promoting
RT complex.";
RL J. Biol. Chem. 272:32011-32018(1997).
RN [8]
RP INTERACTION WITH CDC20.
RX PubMed=9628895; DOI=10.1083/jcb.141.6.1393;
RA Kallio M., Weinstein J., Daum J.R., Burke D.J., Gorbsky G.J.;
RT "Mammalian p55CDC mediates association of the spindle checkpoint protein
RT Mad2 with the cyclosome/anaphase-promoting complex, and is involved in
RT regulating anaphase onset and late mitotic events.";
RL J. Cell Biol. 141:1393-1406(1998).
RN [9]
RP PHOSPHORYLATION AT SER-112; SER-490; SER-560; THR-581; SER-595 AND THR-599.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-581, AND IDENTIFICATION BY
RP 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, AND
RP IDENTIFICATION BY 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-581, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 212-539 IN COMPLEX WITH CDC26, TPR
RP REPEATS, AND SUBUNIT.
RX PubMed=19668213; DOI=10.1038/nsmb.1645;
RA Wang J., Dye B.T., Rajashankar K.R., Kurinov I., Schulman B.A.;
RT "Insights into anaphase promoting complex TPR subdomain assembly from a
RT CDC26-APC6 structure.";
RL Nat. Struct. Mol. Biol. 16:987-989(2009).
RN [20]
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 [21] {ECO:0007744|PDB:4UI9, ECO:0007744|PDB:5A31}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF APC/C, AND SUBUNIT.
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: V-shaped homodimer. The mammalian APC/C is composed at least
CC of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5,
CC CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13,
CC ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains
CC with a combined molecular mass of around 1.2 MDa; APC/C interacts with
CC FZR1 and FBXO5 (PubMed:26083744, PubMed:25043029). Interacts with PPP5C
CC and CDC20 (PubMed:9628895, PubMed:9405394). Interacts with CDC26
CC (PubMed:19668213). {ECO:0000269|PubMed:19668213,
CC ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744,
CC ECO:0000269|PubMed:9405394, ECO:0000269|PubMed:9628895}.
CC -!- INTERACTION:
CC Q13042; Q8NHZ8: CDC26; NbExp=15; IntAct=EBI-994830, EBI-2555941;
CC Q13042; P45984: MAPK9; NbExp=3; IntAct=EBI-994830, EBI-713568;
CC Q13042; Q13148: TARDBP; NbExp=3; IntAct=EBI-994830, EBI-372899;
CC Q13042-1; Q8NHZ8: CDC26; NbExp=5; IntAct=EBI-15798699, EBI-2555941;
CC Q13042-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-10974085, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:7736578}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:7736578}. Note=Colocalizes
CC with CDC27 to the centrosome at all stages of the cell cycle and to the
CC mitotic spindle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13042-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13042-2; Sequence=VSP_008427;
CC Name=3;
CC IsoId=Q13042-3; Sequence=VSP_008427, VSP_008428;
CC Name=4;
CC IsoId=Q13042-4; Sequence=VSP_057270;
CC -!- DOMAIN: TPR repeats 1-7 mediate homodimerization, while the C-terminal
CC TPR repeats bind to CDC26, burying its hydrophobic N-terminus.
CC {ECO:0000269|PubMed:19668213}.
CC -!- PTM: Phosphorylated. Phosphorylation on Ser-560 occurs specifically
CC during mitosis. {ECO:0000269|PubMed:14657031}.
CC -!- SIMILARITY: Belongs to the APC6/CDC16 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc16/";
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DR EMBL; U18291; AAC50200.1; -; mRNA.
DR EMBL; AF164598; AAD45156.1; -; mRNA.
DR EMBL; AY599074; AAS94323.1; -; Genomic_DNA.
DR EMBL; AL160396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX09237.1; -; Genomic_DNA.
DR EMBL; CH471085; EAX09244.1; -; Genomic_DNA.
DR EMBL; CH471085; EAX09245.1; -; Genomic_DNA.
DR EMBL; BC010875; AAH10875.1; -; mRNA.
DR EMBL; BC017244; AAH17244.1; -; mRNA.
DR CCDS; CCDS81786.1; -. [Q13042-2]
DR CCDS; CCDS81787.1; -. [Q13042-4]
DR CCDS; CCDS9542.2; -. [Q13042-1]
DR PIR; A56519; A56519.
DR RefSeq; NP_001072113.1; NM_001078645.2. [Q13042-1]
DR RefSeq; NP_001305446.1; NM_001318517.2. [Q13042-2]
DR RefSeq; NP_001305447.1; NM_001318518.2. [Q13042-3]
DR RefSeq; NP_001317030.1; NM_001330101.1. [Q13042-2]
DR RefSeq; NP_001317033.1; NM_001330104.1. [Q13042-4]
DR RefSeq; NP_001317034.1; NM_001330105.1. [Q13042-4]
DR RefSeq; NP_003894.3; NM_003903.4. [Q13042-1]
DR RefSeq; XP_016876322.1; XM_017020833.1. [Q13042-4]
DR PDB; 3HYM; X-ray; 2.80 A; B/D/F/H/J/L=212-539.
DR PDB; 4UI9; EM; 3.60 A; J/K=1-620.
DR PDB; 5A31; EM; 4.30 A; J/K=1-620.
DR PDB; 5G04; EM; 4.00 A; J/K=1-620.
DR PDB; 5G05; EM; 3.40 A; J/K=1-620.
DR PDB; 5KHR; EM; 6.10 A; J/K=1-620.
DR PDB; 5KHU; EM; 4.80 A; J/K=1-620.
DR PDB; 5L9T; EM; 6.40 A; J/K=1-620.
DR PDB; 5L9U; EM; 6.40 A; J/K=1-620.
DR PDB; 5LCW; EM; 4.00 A; J/K=1-620.
DR PDB; 6Q6G; EM; 3.20 A; K/Q=1-620.
DR PDB; 6Q6H; EM; 3.20 A; K/Q=1-620.
DR PDB; 6TLJ; EM; 3.80 A; J/K=1-620.
DR PDB; 6TM5; EM; 3.90 A; J/K=1-620.
DR PDB; 6TNT; EM; 3.78 A; J/K=1-620.
DR PDB; 7QE7; EM; 2.90 A; K/Q=1-620.
DR PDBsum; 3HYM; -.
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; Q13042; -.
DR SMR; Q13042; -.
DR BioGRID; 114400; 223.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR CORUM; Q13042; -.
DR DIP; DIP-36423N; -.
DR IntAct; Q13042; 148.
DR MINT; Q13042; -.
DR STRING; 9606.ENSP00000353549; -.
DR iPTMnet; Q13042; -.
DR PhosphoSitePlus; Q13042; -.
DR BioMuta; CDC16; -.
DR DMDM; 37537763; -.
DR EPD; Q13042; -.
DR jPOST; Q13042; -.
DR MassIVE; Q13042; -.
DR MaxQB; Q13042; -.
DR PaxDb; Q13042; -.
DR PeptideAtlas; Q13042; -.
DR PRIDE; Q13042; -.
DR ProteomicsDB; 59116; -. [Q13042-1]
DR ProteomicsDB; 59117; -. [Q13042-2]
DR ProteomicsDB; 59118; -. [Q13042-3]
DR ProteomicsDB; 69376; -.
DR Antibodypedia; 11890; 431 antibodies from 40 providers.
DR DNASU; 8881; -.
DR Ensembl; ENST00000252457.9; ENSP00000252457.5; ENSG00000130177.16. [Q13042-2]
DR Ensembl; ENST00000356221.8; ENSP00000348554.3; ENSG00000130177.16. [Q13042-1]
DR Ensembl; ENST00000360383.7; ENSP00000353549.3; ENSG00000130177.16. [Q13042-1]
DR Ensembl; ENST00000375308.5; ENSP00000364457.1; ENSG00000130177.16. [Q13042-4]
DR Ensembl; ENST00000375310.5; ENSP00000364459.1; ENSG00000130177.16. [Q13042-4]
DR GeneID; 8881; -.
DR KEGG; hsa:8881; -.
DR MANE-Select; ENST00000356221.8; ENSP00000348554.3; NM_001078645.3; NP_001072113.1.
DR UCSC; uc001vuk.1; human. [Q13042-1]
DR CTD; 8881; -.
DR DisGeNET; 8881; -.
DR GeneCards; CDC16; -.
DR HGNC; HGNC:1720; CDC16.
DR HPA; ENSG00000130177; Low tissue specificity.
DR MIM; 603461; gene.
DR neXtProt; NX_Q13042; -.
DR OpenTargets; ENSG00000130177; -.
DR PharmGKB; PA26256; -.
DR VEuPathDB; HostDB:ENSG00000130177; -.
DR eggNOG; KOG1173; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_011751_3_2_1; -.
DR InParanoid; Q13042; -.
DR OMA; DPFHNNA; -.
DR PhylomeDB; Q13042; -.
DR TreeFam; TF101054; -.
DR PathwayCommons; Q13042; -.
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; Q13042; -.
DR SIGNOR; Q13042; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8881; 817 hits in 1096 CRISPR screens.
DR ChiTaRS; CDC16; human.
DR EvolutionaryTrace; Q13042; -.
DR GeneWiki; CDC16; -.
DR GenomeRNAi; 8881; -.
DR Pharos; Q13042; Tbio.
DR PRO; PR:Q13042; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q13042; protein.
DR Bgee; ENSG00000130177; Expressed in right uterine tube and 208 other tissues.
DR ExpressionAtlas; Q13042; baseline and differential.
DR Genevisible; Q13042; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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: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:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR DisProt; DP01452; -.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..620
FT /note="Cell division cycle protein 16 homolog"
FT /id="PRO_0000106267"
FT REPEAT 4..33
FT /note="TPR 1"
FT REPEAT 37..62
FT /note="TPR 2"
FT REPEAT 70..93
FT /note="TPR 3"
FT REPEAT 128..159
FT /note="TPR 4"
FT REPEAT 164..187
FT /note="TPR 5"
FT REPEAT 198..222
FT /note="TPR 6"
FT REPEAT 232..260
FT /note="TPR 7"
FT REPEAT 267..294
FT /note="TPR 8"
FT REPEAT 299..329
FT /note="TPR 9"
FT REPEAT 334..362
FT /note="TPR 10"
FT REPEAT 369..397
FT /note="TPR 11"
FT REPEAT 402..434
FT /note="TPR 12"
FT REPEAT 442..474
FT /note="TPR 13"
FT REPEAT 479..508
FT /note="TPR 14"
FT REGION 574..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 581
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 599
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057270"
FT VAR_SEQ 36
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:7736578"
FT /id="VSP_008427"
FT VAR_SEQ 367..417
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_008428"
FT CONFLICT 138
FT /note="K -> Q (in Ref. 1; AAC50200)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="P -> L (in Ref. 2; AAD45156)"
FT /evidence="ECO:0000305"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:6Q6G"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6Q6H"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:3HYM"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 281..294
FT /evidence="ECO:0007829|PDB:3HYM"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:3HYM"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 335..347
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:3HYM"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:3HYM"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 418..432
FT /evidence="ECO:0007829|PDB:3HYM"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:3HYM"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 461..474
FT /evidence="ECO:0007829|PDB:3HYM"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 480..492
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 495..503
FT /evidence="ECO:0007829|PDB:3HYM"
FT TURN 504..508
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 513..524
FT /evidence="ECO:0007829|PDB:3HYM"
FT TURN 525..528
FT /evidence="ECO:0007829|PDB:3HYM"
FT HELIX 555..559
FT /evidence="ECO:0007829|PDB:7QE7"
SQ SEQUENCE 620 AA; 71656 MW; A9C4F24615DF17EB CRC64;
MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT AQYHRAAHAL
RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DVLDMEEPIN KRLFEKYLKD ESGFKDPSSD
WEMSQSSIKS SICLLRGKIY DALDNRTLAT YSYKEALKLD VYCFEAFDLL TSHHMLTAQE
EKELLESLPL SKLCNEEQEL LRFLFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER
HYYNCDFKMC YKLTSVVMEK DPFHASCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV
SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH DQAMAAYFTA
AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FSQALSIAPE DPFVMHEVGV VAFQNGEWKT
AEKWFLDALE KIKAIGNEVT VDKWEPLLNN LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS
TYSAIGYIHS LMGNFENAVD YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD
KLKCYDFDVH TMKTLKNIIS PPWDFREFEV EKQTAEETGL TPLETSRKTP DSRPSLEETF
EIEMNESDMM LETSMSDHST
