APC16_HUMAN
ID APC16_HUMAN Reviewed; 110 AA.
AC Q96DE5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Anaphase-promoting complex subunit 16;
DE Short=APC16;
DE AltName: Full=Cyclosome subunit 16;
GN Name=ANAPC16; Synonyms=C10orf104, CENP-27 {ECO:0000303|PubMed:20813266};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [4]
RP FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20360068; DOI=10.1126/science.1181348;
RA Hutchins J.R., Toyoda Y., Hegemann B., Poser I., Heriche J.K., Sykora M.M.,
RA Augsburg M., Hudecz O., Buschhorn B.A., Bulkescher J., Conrad C.,
RA Comartin D., Schleiffer A., Sarov M., Pozniakovsky A., Slabicki M.M.,
RA Schloissnig S., Steinmacher I., Leuschner M., Ssykor A., Lawo S.,
RA Pelletier L., Stark H., Nasmyth K., Ellenberg J., Durbin R., Buchholz F.,
RA Mechtler K., Hyman A.A., Peters J.M.;
RT "Systematic analysis of human protein complexes identifies chromosome
RT segregation proteins.";
RL Science 328:593-599(2010).
RN [5]
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 [6]
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 [7]
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 [8] {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:20360068}.
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 (PubMed:26083744, PubMed:25043029). ANAPC16 associates with
CC the rest of the complex independently of ANAPC2 and ANAPC11.
CC {ECO:0000269|PubMed:20360068, ECO:0000269|PubMed:25043029,
CC ECO:0000269|PubMed:26083744}.
CC -!- INTERACTION:
CC Q96DE5; O75031: HSF2BP; NbExp=3; IntAct=EBI-2555937, EBI-7116203;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20360068}. Nucleus
CC {ECO:0000269|PubMed:20360068}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:20813266}.
CC -!- SIMILARITY: Belongs to the APC16 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL607035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009530; AAH09530.1; -; mRNA.
DR CCDS; CCDS7314.1; -.
DR RefSeq; NP_001229475.1; NM_001242546.1.
DR RefSeq; NP_001229476.1; NM_001242547.1.
DR RefSeq; NP_775744.1; NM_173473.3.
DR PDB; 4RG6; X-ray; 3.30 A; S=74-109.
DR PDB; 4RG9; X-ray; 3.25 A; S=74-109.
DR PDB; 4UI9; EM; 3.60 A; E=1-110.
DR PDB; 5A31; EM; 4.30 A; E=1-110.
DR PDB; 5G04; EM; 4.00 A; E=1-110.
DR PDB; 5G05; EM; 3.40 A; E=1-110.
DR PDB; 5KHR; EM; 6.10 A; E=1-110.
DR PDB; 5KHU; EM; 4.80 A; E=1-110.
DR PDB; 5L9T; EM; 6.40 A; E=1-110.
DR PDB; 5L9U; EM; 6.40 A; E=1-110.
DR PDB; 5LCW; EM; 4.00 A; E=1-110.
DR PDB; 6Q6G; EM; 3.20 A; H=1-110.
DR PDB; 6Q6H; EM; 3.20 A; H=1-110.
DR PDB; 6TLJ; EM; 3.80 A; E=1-110.
DR PDB; 6TM5; EM; 3.90 A; E=1-110.
DR PDB; 6TNT; EM; 3.78 A; E=1-110.
DR PDB; 7QE7; EM; 2.90 A; H=1-110.
DR PDBsum; 4RG6; -.
DR PDBsum; 4RG9; -.
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; Q96DE5; -.
DR SMR; Q96DE5; -.
DR BioGRID; 125643; 82.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR DIP; DIP-56449N; -.
DR IntAct; Q96DE5; 34.
DR MINT; Q96DE5; -.
DR STRING; 9606.ENSP00000477760; -.
DR iPTMnet; Q96DE5; -.
DR MetOSite; Q96DE5; -.
DR PhosphoSitePlus; Q96DE5; -.
DR BioMuta; ANAPC16; -.
DR EPD; Q96DE5; -.
DR jPOST; Q96DE5; -.
DR MassIVE; Q96DE5; -.
DR MaxQB; Q96DE5; -.
DR PaxDb; Q96DE5; -.
DR PeptideAtlas; Q96DE5; -.
DR PRIDE; Q96DE5; -.
DR ProteomicsDB; 76284; -.
DR Antibodypedia; 48879; 10 antibodies from 7 providers.
DR DNASU; 119504; -.
DR Ensembl; ENST00000299381.5; ENSP00000299381.3; ENSG00000166295.9.
DR Ensembl; ENST00000621663.4; ENSP00000477760.1; ENSG00000166295.9.
DR GeneID; 119504; -.
DR KEGG; hsa:119504; -.
DR MANE-Select; ENST00000299381.5; ENSP00000299381.3; NM_173473.4; NP_775744.1.
DR UCSC; uc001jsv.4; human.
DR CTD; 119504; -.
DR DisGeNET; 119504; -.
DR GeneCards; ANAPC16; -.
DR HGNC; HGNC:26976; ANAPC16.
DR HPA; ENSG00000166295; Low tissue specificity.
DR MIM; 613427; gene.
DR neXtProt; NX_Q96DE5; -.
DR OpenTargets; ENSG00000166295; -.
DR PharmGKB; PA165548225; -.
DR VEuPathDB; HostDB:ENSG00000166295; -.
DR eggNOG; ENOG502RZ50; Eukaryota.
DR GeneTree; ENSGT00390000018109; -.
DR HOGENOM; CLU_153312_0_0_1; -.
DR InParanoid; Q96DE5; -.
DR OMA; XGSERFL; -.
DR OrthoDB; 1642213at2759; -.
DR PhylomeDB; Q96DE5; -.
DR TreeFam; TF332754; -.
DR PathwayCommons; Q96DE5; -.
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 SignaLink; Q96DE5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 119504; 13 hits in 1082 CRISPR screens.
DR ChiTaRS; ANAPC16; human.
DR GenomeRNAi; 119504; -.
DR Pharos; Q96DE5; Tdark.
DR PRO; PR:Q96DE5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96DE5; protein.
DR Bgee; ENSG00000166295; Expressed in parotid gland and 194 other tissues.
DR ExpressionAtlas; Q96DE5; baseline and differential.
DR Genevisible; Q96DE5; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IC:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
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; DP01455; -.
DR InterPro; IPR029641; APC16.
DR PANTHER; PTHR31564; PTHR31564; 1.
DR Pfam; PF17256; ANAPC16; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Kinetochore; Mitosis; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..110
FT /note="Anaphase-promoting complex subunit 16"
FT /id="PRO_0000089816"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 52..84
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 85..91
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6Q6H"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:7QE7"
SQ SEQUENCE 110 AA; 11667 MW; F348FA92F4B89E4F CRC64;
MAASSSSSSA GGVSGSSVTG SGFSVSDLAP PRKALFTYPK GAGEMLEDGS ERFLCESVFS
YQVASTLKQV KHDQQVARME KLAGLVEELE ADEWRFKPIE QLLGFTPSSG
