GenomeNet

Database: UniProt
Entry: Q13042
LinkDB: Q13042
Original site: Q13042 
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   17-JUN-2020, entry version 191.
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:0000244|PDB:4UI9, ECO:0000244|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       Q13042-1; Q8NHZ8: CDC26; NbExp=5; IntAct=EBI-15798699, EBI-2555941;
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/";
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   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   SMR; Q13042; -.
DR   BioGRID; 114400; 193.
DR   CORUM; Q13042; -.
DR   DIP; DIP-36423N; -.
DR   IntAct; Q13042; 147.
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; 399 antibodies.
DR   DNASU; 8881; -.
DR   Ensembl; ENST00000252457; ENSP00000252457; ENSG00000130177. [Q13042-2]
DR   Ensembl; ENST00000356221; ENSP00000348554; ENSG00000130177. [Q13042-1]
DR   Ensembl; ENST00000360383; ENSP00000353549; ENSG00000130177. [Q13042-1]
DR   Ensembl; ENST00000375308; ENSP00000364457; ENSG00000130177. [Q13042-4]
DR   Ensembl; ENST00000375310; ENSP00000364459; ENSG00000130177. [Q13042-4]
DR   GeneID; 8881; -.
DR   KEGG; hsa:8881; -.
DR   UCSC; uc001vuk.1; human. [Q13042-1]
DR   CTD; 8881; -.
DR   DisGeNET; 8881; -.
DR   EuPathDB; HostDB:ENSG00000130177.14; -.
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   eggNOG; KOG1173; Eukaryota.
DR   eggNOG; ENOG410XNY1; LUCA.
DR   GeneTree; ENSGT00950000182950; -.
DR   HOGENOM; CLU_011751_3_2_1; -.
DR   InParanoid; Q13042; -.
DR   KO; K03353; -.
DR   OMA; QFIDMRR; -.
DR   PhylomeDB; Q13042; -.
DR   TreeFam; TF101054; -.
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; Q13042; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 8881; 750 hits in 793 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 229 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:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   DisProt; DP01452; -.
DR   InterPro; IPR013026; TPR-contain_dom.
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   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:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:14657031"
FT   MOD_RES         581
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:14657031"
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           3..15
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           19..32
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           37..49
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           53..61
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            62..64
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            66..68
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           70..82
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           86..92
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           129..142
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           146..159
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           164..170
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          171..174
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           178..187
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           195..209
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          222..224
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           226..229
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            231..233
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   HELIX           234..243
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           247..260
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   TURN            265..267
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           268..278
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           281..294
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   STRAND          296..298
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           300..311
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           316..327
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   TURN            330..332
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           335..347
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           350..363
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   TURN            364..366
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           369..380
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           384..395
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           402..414
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           418..432
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   TURN            433..435
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   TURN            440..443
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           446..457
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           461..474
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   STRAND          475..477
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           480..492
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           495..503
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   TURN            504..508
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           513..524
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   TURN            525..528
FT                   /evidence="ECO:0000244|PDB:3HYM"
FT   HELIX           556..559
FT                   /evidence="ECO:0000244|PDB:6Q6G"
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
//
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