GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Cell division cycle protein 16 homolog (Anaphase-promoting complex subunit 6) (APC6) (CDC16 homolog) (CDC16Hs) (Cyclosome subunit 6)

 CDC16_HUMAN             Reviewed;         620 AA.
Q13042; A2A365; Q5T8C8; Q7Z651; Q96AE6; Q9Y564;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
03-OCT-2003, sequence version 2.
12-AUG-2020, entry version 192.
RecName: Full=Cell division cycle protein 16 homolog;
AltName: Full=Anaphase-promoting complex subunit 6;
Short=APC6;
AltName: Full=CDC16 homolog;
Short=CDC16Hs;
AltName: Full=Cyclosome subunit 6;
Name=CDC16; Synonyms=ANAPC6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=7736578; DOI=10.1016/0092-8674(95)90336-4;
Tugendreich S., Tomkiel J., Earnshaw W., Hieter P.;
"CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic spindle and
is essential for the metaphase to anaphase transition.";
Cell 81:261-268(1995).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 3).
Zhou P.K., Rigaud O.;
"The differential splicing variants of human CDC16 mRNA.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH PPP5C.
PubMed=9405394; DOI=10.1074/jbc.272.51.32011;
Ollendorff V., Donoghue D.J.;
"The serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two
tetratricopeptide repeat-containing subunits of the anaphase-promoting
complex.";
J. Biol. Chem. 272:32011-32018(1997).
[8]
INTERACTION WITH CDC20.
PubMed=9628895; DOI=10.1083/jcb.141.6.1393;
Kallio M., Weinstein J., Daum J.R., Burke D.J., Gorbsky G.J.;
"Mammalian p55CDC mediates association of the spindle checkpoint protein
Mad2 with the cyclosome/anaphase-promoting complex, and is involved in
regulating anaphase onset and late mitotic events.";
J. Cell Biol. 141:1393-1406(1998).
[9]
PHOSPHORYLATION AT SER-112; SER-490; SER-560; THR-581; SER-595 AND THR-599.
PubMed=14657031; DOI=10.1093/emboj/cdg627;
Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,
Peters J.-M.;
"Mitotic regulation of the human anaphase-promoting complex by
phosphorylation.";
EMBO J. 22:6598-6609(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-581, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
FUNCTION OF THE APC/C.
PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
"Mechanism of ubiquitin-chain formation by the human anaphase-promoting
complex.";
Cell 133:653-665(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-581, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
STRUCTURE BY ELECTRON MICROSCOPY OF THE APC/C.
PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
Engel A., Peters J.-M., Stark H.;
"Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
cryo-electron microscopy model of vertebrate APC/C.";
Mol. Cell 20:867-879(2005).
[19]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 212-539 IN COMPLEX WITH CDC26, TPR
REPEATS, AND SUBUNIT.
PubMed=19668213; DOI=10.1038/nsmb.1645;
Wang J., Dye B.T., Rajashankar K.R., Kurinov I., Schulman B.A.;
"Insights into anaphase promoting complex TPR subdomain assembly from a
CDC26-APC6 structure.";
Nat. Struct. Mol. Biol. 16:987-989(2009).
[20]
STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, AND SUBUNIT.
PubMed=25043029; DOI=10.1038/nature13543;
Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
"Molecular architecture and mechanism of the anaphase-promoting complex.";
Nature 513:388-393(2014).
[21] {ECO:0000244|PDB:4UI9, ECO:0000244|PDB:5A31}
STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF APC/C, AND SUBUNIT.
PubMed=26083744; DOI=10.1038/nature14471;
Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
"Atomic structure of the APC/C and its mechanism of protein
ubiquitination.";
Nature 522:450-454(2015).
-!- FUNCTION: Component of the anaphase promoting complex/cyclosome
(APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
progression through mitosis and the G1 phase of the cell cycle. The
APC/C complex acts by mediating ubiquitination and subsequent
degradation of target proteins: it mainly mediates the formation of
'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
{ECO:0000269|PubMed:18485873}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: V-shaped homodimer. The mammalian APC/C is composed at least
of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5,
CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13,
ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains
with a combined molecular mass of around 1.2 MDa; APC/C interacts with
FZR1 and FBXO5 (PubMed:26083744, PubMed:25043029). Interacts with PPP5C
and CDC20 (PubMed:9628895, PubMed:9405394). Interacts with CDC26
(PubMed:19668213). {ECO:0000269|PubMed:19668213,
ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744,
ECO:0000269|PubMed:9405394, ECO:0000269|PubMed:9628895}.
-!- INTERACTION:
Q13042; Q8NHZ8: CDC26; NbExp=15; IntAct=EBI-994830, EBI-2555941;
Q13042; P45984: MAPK9; NbExp=3; IntAct=EBI-994830, EBI-713568;
Q13042-1; Q8NHZ8: CDC26; NbExp=5; IntAct=EBI-15798699, EBI-2555941;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000269|PubMed:7736578}. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:7736578}. Note=Colocalizes
with CDC27 to the centrosome at all stages of the cell cycle and to the
mitotic spindle.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q13042-1; Sequence=Displayed;
Name=2;
IsoId=Q13042-2; Sequence=VSP_008427;
Name=3;
IsoId=Q13042-3; Sequence=VSP_008427, VSP_008428;
Name=4;
IsoId=Q13042-4; Sequence=VSP_057270;
-!- DOMAIN: TPR repeats 1-7 mediate homodimerization, while the C-terminal
TPR repeats bind to CDC26, burying its hydrophobic N-terminus.
{ECO:0000269|PubMed:19668213}.
-!- PTM: Phosphorylated. Phosphorylation on Ser-560 occurs specifically
during mitosis. {ECO:0000269|PubMed:14657031}.
-!- SIMILARITY: Belongs to the APC6/CDC16 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc16/";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; U18291; AAC50200.1; -; mRNA.
EMBL; AF164598; AAD45156.1; -; mRNA.
EMBL; AY599074; AAS94323.1; -; Genomic_DNA.
EMBL; AL160396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471085; EAX09237.1; -; Genomic_DNA.
EMBL; CH471085; EAX09244.1; -; Genomic_DNA.
EMBL; CH471085; EAX09245.1; -; Genomic_DNA.
EMBL; BC010875; AAH10875.1; -; mRNA.
EMBL; BC017244; AAH17244.1; -; mRNA.
CCDS; CCDS81786.1; -. [Q13042-2]
CCDS; CCDS81787.1; -. [Q13042-4]
CCDS; CCDS9542.2; -. [Q13042-1]
PIR; A56519; A56519.
RefSeq; NP_001072113.1; NM_001078645.2. [Q13042-1]
RefSeq; NP_001305446.1; NM_001318517.2. [Q13042-2]
RefSeq; NP_001305447.1; NM_001318518.2. [Q13042-3]
RefSeq; NP_001317030.1; NM_001330101.1. [Q13042-2]
RefSeq; NP_001317033.1; NM_001330104.1. [Q13042-4]
RefSeq; NP_001317034.1; NM_001330105.1. [Q13042-4]
RefSeq; NP_003894.3; NM_003903.4. [Q13042-1]
RefSeq; XP_016876322.1; XM_017020833.1. [Q13042-4]
PDB; 3HYM; X-ray; 2.80 A; B/D/F/H/J/L=212-539.
PDB; 4UI9; EM; 3.60 A; J/K=1-620.
PDB; 5A31; EM; 4.30 A; J/K=1-620.
PDB; 5G04; EM; 4.00 A; J/K=1-620.
PDB; 5G05; EM; 3.40 A; J/K=1-620.
PDB; 5KHR; EM; 6.10 A; J/K=1-620.
PDB; 5KHU; EM; 4.80 A; J/K=1-620.
PDB; 5L9T; EM; 6.40 A; J/K=1-620.
PDB; 5L9U; EM; 6.40 A; J/K=1-620.
PDB; 5LCW; EM; 4.00 A; J/K=1-620.
PDB; 6Q6G; EM; 3.20 A; K/Q=1-620.
PDB; 6Q6H; EM; 3.20 A; K/Q=1-620.
PDB; 6TLJ; EM; 3.80 A; J/K=1-620.
PDB; 6TM5; EM; 3.90 A; J/K=1-620.
PDBsum; 3HYM; -.
PDBsum; 4UI9; -.
PDBsum; 5A31; -.
PDBsum; 5G04; -.
PDBsum; 5G05; -.
PDBsum; 5KHR; -.
PDBsum; 5KHU; -.
PDBsum; 5L9T; -.
PDBsum; 5L9U; -.
PDBsum; 5LCW; -.
PDBsum; 6Q6G; -.
PDBsum; 6Q6H; -.
PDBsum; 6TLJ; -.
PDBsum; 6TM5; -.
SMR; Q13042; -.
BioGRID; 114400; 196.
CORUM; Q13042; -.
DIP; DIP-36423N; -.
IntAct; Q13042; 147.
MINT; Q13042; -.
STRING; 9606.ENSP00000353549; -.
iPTMnet; Q13042; -.
PhosphoSitePlus; Q13042; -.
BioMuta; CDC16; -.
DMDM; 37537763; -.
EPD; Q13042; -.
jPOST; Q13042; -.
MassIVE; Q13042; -.
MaxQB; Q13042; -.
PaxDb; Q13042; -.
PeptideAtlas; Q13042; -.
PRIDE; Q13042; -.
ProteomicsDB; 59116; -. [Q13042-1]
ProteomicsDB; 59117; -. [Q13042-2]
ProteomicsDB; 59118; -. [Q13042-3]
ProteomicsDB; 69376; -.
Antibodypedia; 11890; 401 antibodies.
DNASU; 8881; -.
Ensembl; ENST00000252457; ENSP00000252457; ENSG00000130177. [Q13042-2]
Ensembl; ENST00000356221; ENSP00000348554; ENSG00000130177. [Q13042-1]
Ensembl; ENST00000360383; ENSP00000353549; ENSG00000130177. [Q13042-1]
Ensembl; ENST00000375308; ENSP00000364457; ENSG00000130177. [Q13042-4]
Ensembl; ENST00000375310; ENSP00000364459; ENSG00000130177. [Q13042-4]
GeneID; 8881; -.
KEGG; hsa:8881; -.
UCSC; uc001vuk.1; human. [Q13042-1]
CTD; 8881; -.
DisGeNET; 8881; -.
EuPathDB; HostDB:ENSG00000130177.14; -.
GeneCards; CDC16; -.
HGNC; HGNC:1720; CDC16.
HPA; ENSG00000130177; Low tissue specificity.
MIM; 603461; gene.
neXtProt; NX_Q13042; -.
OpenTargets; ENSG00000130177; -.
PharmGKB; PA26256; -.
eggNOG; KOG1173; Eukaryota.
GeneTree; ENSGT00950000182950; -.
HOGENOM; CLU_011751_3_2_1; -.
InParanoid; Q13042; -.
KO; K03353; -.
OMA; QFIDMRR; -.
PhylomeDB; Q13042; -.
TreeFam; TF101054; -.
PathwayCommons; Q13042; -.
Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q13042; -.
UniPathway; UPA00143; -.
BioGRID-ORCS; 8881; 776 hits in 879 CRISPR screens.
ChiTaRS; CDC16; human.
EvolutionaryTrace; Q13042; -.
GeneWiki; CDC16; -.
GenomeRNAi; 8881; -.
Pharos; Q13042; Tbio.
PRO; PR:Q13042; -.
Proteomes; UP000005640; Chromosome 13.
RNAct; Q13042; protein.
Bgee; ENSG00000130177; Expressed in right uterine tube and 241 other tissues.
ExpressionAtlas; Q13042; baseline and differential.
Genevisible; Q13042; HS.
GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
GO; GO:0051301; P:cell division; IBA:GO_Central.
GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome.
DisProt; DP01452; -.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
SMART; SM00028; TPR; 6.
SUPFAM; SSF48452; SSF48452; 2.
PROSITE; PS50005; TPR; 5.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome; Repeat;
TPR repeat; Ubl conjugation pathway.
CHAIN 1..620
/note="Cell division cycle protein 16 homolog"
/id="PRO_0000106267"
REPEAT 4..33
/note="TPR 1"
REPEAT 37..62
/note="TPR 2"
REPEAT 70..93
/note="TPR 3"
REPEAT 128..159
/note="TPR 4"
REPEAT 164..187
/note="TPR 5"
REPEAT 198..222
/note="TPR 6"
REPEAT 232..260
/note="TPR 7"
REPEAT 267..294
/note="TPR 8"
REPEAT 299..329
/note="TPR 9"
REPEAT 334..362
/note="TPR 10"
REPEAT 369..397
/note="TPR 11"
REPEAT 402..434
/note="TPR 12"
REPEAT 442..474
/note="TPR 13"
REPEAT 479..508
/note="TPR 14"
MOD_RES 112
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:14657031"
MOD_RES 490
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:14657031"
MOD_RES 560
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14657031"
MOD_RES 581
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14657031"
MOD_RES 595
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:14657031"
MOD_RES 599
/note="Phosphothreonine"
/evidence="ECO:0000269|PubMed:14657031"
VAR_SEQ 1..94
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_057270"
VAR_SEQ 36
/note="Missing (in isoform 2 and isoform 3)"
/evidence="ECO:0000303|PubMed:7736578"
/id="VSP_008427"
VAR_SEQ 367..417
/note="Missing (in isoform 3)"
/evidence="ECO:0000305"
/id="VSP_008428"
CONFLICT 138
/note="K -> Q (in Ref. 1; AAC50200)"
/evidence="ECO:0000305"
CONFLICT 299
/note="P -> L (in Ref. 2; AAD45156)"
/evidence="ECO:0000305"
HELIX 3..15
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 19..32
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 37..49
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 53..61
/evidence="ECO:0000244|PDB:6Q6G"
TURN 62..64
/evidence="ECO:0000244|PDB:6Q6G"
TURN 66..68
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 70..82
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 86..92
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 129..142
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 146..159
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 164..170
/evidence="ECO:0000244|PDB:6Q6G"
STRAND 171..174
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 178..187
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 195..209
/evidence="ECO:0000244|PDB:6Q6G"
STRAND 222..224
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 226..229
/evidence="ECO:0000244|PDB:6Q6G"
TURN 231..233
/evidence="ECO:0000244|PDB:6Q6H"
HELIX 234..243
/evidence="ECO:0000244|PDB:3HYM"
HELIX 247..260
/evidence="ECO:0000244|PDB:3HYM"
TURN 265..267
/evidence="ECO:0000244|PDB:3HYM"
HELIX 268..278
/evidence="ECO:0000244|PDB:3HYM"
HELIX 281..294
/evidence="ECO:0000244|PDB:3HYM"
STRAND 296..298
/evidence="ECO:0000244|PDB:5G05"
HELIX 300..311
/evidence="ECO:0000244|PDB:3HYM"
HELIX 316..327
/evidence="ECO:0000244|PDB:3HYM"
TURN 330..332
/evidence="ECO:0000244|PDB:5G05"
HELIX 335..347
/evidence="ECO:0000244|PDB:3HYM"
HELIX 350..363
/evidence="ECO:0000244|PDB:3HYM"
TURN 364..366
/evidence="ECO:0000244|PDB:3HYM"
HELIX 369..380
/evidence="ECO:0000244|PDB:3HYM"
HELIX 384..395
/evidence="ECO:0000244|PDB:3HYM"
HELIX 402..414
/evidence="ECO:0000244|PDB:3HYM"
HELIX 418..432
/evidence="ECO:0000244|PDB:3HYM"
TURN 433..435
/evidence="ECO:0000244|PDB:3HYM"
TURN 440..443
/evidence="ECO:0000244|PDB:3HYM"
HELIX 446..457
/evidence="ECO:0000244|PDB:3HYM"
HELIX 461..474
/evidence="ECO:0000244|PDB:3HYM"
STRAND 475..477
/evidence="ECO:0000244|PDB:6Q6G"
HELIX 480..492
/evidence="ECO:0000244|PDB:3HYM"
HELIX 495..503
/evidence="ECO:0000244|PDB:3HYM"
TURN 504..508
/evidence="ECO:0000244|PDB:3HYM"
HELIX 513..524
/evidence="ECO:0000244|PDB:3HYM"
TURN 525..528
/evidence="ECO:0000244|PDB:3HYM"
HELIX 556..559
/evidence="ECO:0000244|PDB:6Q6G"
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


Related products :

Catalog number Product name Quantity
EIAAB06421 ANAPC6,Anaphase-promoting complex subunit 6,APC6,CDC16,CDC16 homolog,CDC16Hs,Cell division cycle protein 16 homolog,Cyclosome subunit 6,Homo sapiens,Human
EIAAB06420 Anapc6,Anaphase-promoting complex subunit 6,APC6,Cdc16,Cell division cycle protein 16 homolog,Cyclosome subunit 6,Mouse,Mus musculus
E1771b ELISA ANAPC8,Anaphase-promoting complex subunit 8,APC8,Bos taurus,Bovine,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8 96T
E1771m ELISA Anapc8,Anaphase-promoting complex subunit 8,APC8,Cdc23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Mouse,Mus musculus 96T
E1771m ELISA kit Anapc8,Anaphase-promoting complex subunit 8,APC8,Cdc23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Mouse,Mus musculus 96T
U1771m CLIA Anapc8,Anaphase-promoting complex subunit 8,APC8,Cdc23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Mouse,Mus musculus 96T
E1771b ELISA kit ANAPC8,Anaphase-promoting complex subunit 8,APC8,Bos taurus,Bovine,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8 96T
U1771b CLIA ANAPC8,Anaphase-promoting complex subunit 8,APC8,Bos taurus,Bovine,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8 96T
E1771h ELISA kit ANAPC8,Anaphase-promoting complex subunit 8,APC8,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Homo sapiens,Human 96T
U1771h CLIA ANAPC8,Anaphase-promoting complex subunit 8,APC8,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Homo sapiens,Human 96T
E1771h ELISA ANAPC8,Anaphase-promoting complex subunit 8,APC8,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Homo sapiens,Human 96T
EIAAB06428 ANAPC12,Anaphase-promoting complex subunit 12,Anaphase-promoting complex subunit CDC26,APC12,C9orf17,CDC26,Cell division cycle protein 26 homolog,Homo sapiens,Human
EIAAB06432 ANAPC3,Anaphase-promoting complex subunit 3,APC3,CDC27,CDC27 homolog,CDC27Hs,Cell division cycle protein 27 homolog,D0S1430E,D17S978E,H-NUC,Homo sapiens,Human
EIAAB06426 Anaphase-promoting complex subunit CDC26,Cdc26,Cell division cycle protein 26 homolog,Mouse,Mus musculus
EIAAB06427 Anaphase-promoting complex subunit CDC26,Bos taurus,Bovine,CDC26,Cell division cycle protein 26 homolog
EIAAB06429 Anaphase-promoting complex subunit CDC26,Cdc26,Cell division cycle protein 26 homolog,Protein BWK-2,Rat,Rattus norvegicus
29-605 The anaphase-promoting complex (APC) consists of at least 8 protein subunits, including APC5, CDC27 (APC3), CDC16 (APC6), and CDC23 (APC8).The anaphase-promoting complex (APC) consists of at least 8 p 0.05 mg
CSB-EL004988MO Mouse Cell division cycle protein 16 homolog(CDC16) ELISA kit 96T
CSB-EL004988HU Human Cell division cycle protein 16 homolog(CDC16) ELISA kit 96T
CSB-EL004988MO Mouse Cell division cycle protein 16 homolog(CDC16) ELISA kit SpeciesMouse 96T
CSB-EL004988HU Human Cell division cycle protein 16 homolog(CDC16) ELISA kit SpeciesHuman 96T
CDC16_MOUSE ELISA Kit FOR Cell division cycle protein 16 homolog; organism: Mouse; gene name: Cdc16 96T
CDC16_HUMAN ELISA Kit FOR Cell division cycle protein 16 homolog; organism: Human; gene name: CDC16 96T
201-20-0954 CDC16{cell division cycle 16 homolog (S. cerevisiae)}rabbit.pAb 0.1ml
CDC20B CDC16 Gene cell division cycle 16 homolog (S. cerevisiae)
Pathways :
WP1566: Citrate cycle (TCA cycle)
WP2272: Pathogenic Escherichia coli infection
WP414: Cell Cycle and Cell Division
WP1694: Pyrimidine metabolism
WP1693: Purine metabolism
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1644: DNA replication
WP2292: Chemokine signaling pathway
WP1634: Butanoate metabolism
WP1411: Cell Division: First embryonic mitosis
WP1680: Oxidative phosphorylation
WP45: G1 to S cell cycle control
WP1078: G1 to S cell cycle control
WP959: G1 to S cell cycle control
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP844: Cell cycle
WP1775: Cell Cycle Checkpoints
WP190: Cell cycle
WP1393: Cell cycle
WP445: G1 to S cell cycle control
WP1626: Benzoate degradation via CoA ligation
WP1792: Cell Cycle, Mitotic
WP1200: Cell cycle
WP1711: Trinitrotoluene degradation

Related Genes :
[APC6 CDC16 At1g78770 F9K20.19] Anaphase-promoting complex subunit 6 (Cell division cycle protein 16 homolog) (CDC16 homolog) (Cyclosome subunit 6) (Protein NOMEGA)
[mat-3 apc-8 cdc-23 pod-4 vex-2 F10C5.1] Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Metaphase-to-anaphase transition defect protein 3)
[ANAPC7 APC7] Anaphase-promoting complex subunit 7 (APC7) (Cyclosome subunit 7)
[APC8 CDC23 At3g48150 T24C20.30] Anaphase-promoting complex subunit 8 (Cell division cycle protein 23 homolog) (CDC23 homolog) (Cyclosome subunit 8)
[cdc-48.1 C06A1.1] Transitional endoplasmic reticulum ATPase homolog 1 (EC 3.6.4.6) (Cell division cycle-related protein 48.1) (p97/CDC48 homolog 1)
[Cdc42] Cell division control protein 42 homolog (EC 3.6.5.2) (G25K GTP-binding protein)
[cdc-48.2 C41C4.8] Transitional endoplasmic reticulum ATPase homolog 2 (EC 3.6.4.6) (Cell division cycle-related protein 48.2) (p97/CDC48 homolog 2)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[mat-2 apc-1 evl-22 pod-3 W10C6.1] Anaphase-promoting complex subunit 1 (APC1) (Metaphase-to-anaphase transition protein 2)
[nuc2 apc3 SPAC17C9.01c SPAC1851.01] Anaphase-promoting complex subunit 3 (20S cyclosome/APC complex protein apc3) (Nuclear alteration protein 2) (Nuclear scaffold-like protein p76)
[APC2 At2g04660 F28I8.30] Anaphase-promoting complex subunit 2 (Cyclosome subunit 2)
[cut4 apc1 SPBC106.09] Anaphase-promoting complex subunit 1 (20S cyclosome/APC complex protein apc1) (Cell untimely torn protein 4)
[Sirt2 Sir2l2] NAD-dependent protein deacetylase sirtuin-2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2) (mSIR2L2)
[APC10 At2g18290 T30D6.20] Anaphase-promoting complex subunit 10 (APC10) (Cyclosome subunit 10)
[CDC42] Cell division control protein 42 homolog (EC 3.6.5.2) (G25K GTP-binding protein)
[CDC48 YDL126C] Cell division control protein 48 (EC 3.6.4.6) (Cell division cycle protein 48) (Transitional endoplasmic reticulum ATPase homolog)
[Dtl Cdt2 L2dtl Ramp] Denticleless protein homolog (Lethal(2) denticleless protein homolog) (Meth A retinoic acid-regulated nuclear matrix-associated protein) (Meth A RAMP) (Retinoic acid-regulated nuclear matrix-associated protein)
[CDC14A] Dual specificity protein phosphatase CDC14A (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog A)
[cdc16 bub2 SPAC6F6.08c] Cell division control protein 16
[cdc-48.3 K04G2.3] ATPase family protein 2 homolog (EC 3.6.4.10) (Cell division cycle-related protein 48.3)
[CDC6 CDC18L] Cell division control protein 6 homolog (CDC6-related protein) (Cdc18-related protein) (HsCdc18) (p62(cdc6)) (HsCDC6)
[cut20 apc4 lid1 SPAC19G12.01c SPAPJ698.04c] Anaphase-promoting complex subunit 4 (20S cyclosome/APC complex protein apc4) (Cell untimely torn protein 20)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdc42] Cell division control protein 42 homolog (EC 3.6.5.2)
[CDC42] Cell division control protein 42 homolog (EC 3.6.5.2)
[CDC42] Cell division control protein 42 homolog (EC 3.6.5.2) (G25K GTP-binding protein)
[apc-11 F35G12.9] Anaphase-promoting complex subunit 11 (APC11)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)
[Cops2 Csn2 Trip15] COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)

Bibliography :