ID ANC2_HUMAN Reviewed; 822 AA. AC Q9UJX6; Q5VSG1; Q96DG5; Q96GG4; Q9P2E1; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 13-SEP-2023, entry version 199. DE RecName: Full=Anaphase-promoting complex subunit 2; DE Short=APC2; DE AltName: Full=Cyclosome subunit 2; GN Name=ANAPC2; Synonyms=APC2, KIAA1406; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CULLIN HOMOLOGY REGION, AND RP SUBUNIT. RX PubMed=9469815; DOI=10.1126/science.279.5354.1219; RA Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.; RT "Identification of a cullin homology region in a subunit of the anaphase- RT promoting complex."; RL Science 279:1219-1222(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 243-822 (ISOFORM 2). RC TISSUE=Brain, Cervix, and Ovary; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-822 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [5] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [6] RP FUNCTION, AND INTERACTION WITH ANAPC11 AND UBCH10. RX PubMed=11739784; DOI=10.1091/mbc.12.12.3839; RA Tang Z., Li B., Bharadwaj R., Zhu H., Oezkan E., Hakala K., Deisenhofer J., RA Yu H.; RT "APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin RT ligase module of the anaphase-promoting complex."; RL Mol. Biol. Cell 12:3839-3851(2001). RN [7] RP PHOSPHORYLATION AT SER-314 AND SER-534. 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND SER-314, 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-470 AND SER-534, AND 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, 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 [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-314 AND SER-534, 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 [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP 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 [18] 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 [19] {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). RN [20] {ECO:0007744|PDB:5L9T, ECO:0007744|PDB:5L9U} RP STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) IN COMPLEX WITH APC/C; RP UBE2C AND UBE2S, INTERACTION WITH UBE2C AND UBE2S, AND MUTAGENESIS OF RP ASP-350 AND ASP-353. RX PubMed=27259151; DOI=10.1016/j.cell.2016.05.037; RA Brown N.G., VanderLinden R., Watson E.R., Weissmann F., Ordureau A., RA Wu K.P., Zhang W., Yu S., Mercredi P.Y., Harrison J.S., Davidson I.F., RA Qiao R., Lu Y., Dube P., Brunner M.R., Grace C.R., Miller D.J., RA Haselbach D., Jarvis M.A., Yamaguchi M., Yanishevski D., Petzold G., RA Sidhu S.S., Kuhlman B., Kirschner M.W., Harper J.W., Peters J.M., Stark H., RA Schulman B.A.; RT "Dual RING E3 architectures regulate multiubiquitination and ubiquitin RT chain elongation by APC/C."; RL Cell 165:1440-1453(2016). RN [21] RP INTERACTION WITH FBXO43. RX PubMed=34595750; DOI=10.1111/cge.14069; RA Wu H., Zhang X., Shen Q., Liu Y., Gao Y., Wang G., Lv M., Hua R., Xu Y., RA Zhou P., Wei Z., Tao F., He X., Cao Y., Liu M.; RT "A homozygous loss-of-function mutation in FBXO43 causes human non- RT obstructive azoospermia."; RL Clin. Genet. 101:55-64(2022). CC -!- FUNCTION: Together with the RING-H2 protein ANAPC11, constitutes the CC catalytic 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. The CC CDC20-APC/C complex positively regulates the formation of synaptic CC vesicle clustering at active zone to the presynaptic membrane in CC postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives CC presynaptic differentiation. {ECO:0000269|PubMed:11739784, CC ECO:0000269|PubMed:18485873}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and CC ANAPC16 that assemble into a complex of at least 19 chains with a CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 CC and FBXO5 (PubMed:25043029, PubMed:26083744). In the context of the CC APC/C complex, directly interacts with UBE2C and UBE2S CC (PubMed:27259151). Interacts (via cullin domain) with ANAPC11 and with CC UBCH10 (PubMed:11739784). Interacts with NEUROD2 (By similarity). CC Interacts with FBXO43; the interaction is direct. CC {ECO:0000250|UniProtKB:Q8BZQ7, ECO:0000269|PubMed:11739784, CC ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744, CC ECO:0000269|PubMed:27259151, ECO:0000269|PubMed:34595750}. CC -!- INTERACTION: CC Q9UJX6; Q9UKT4-1: FBXO5; NbExp=7; IntAct=EBI-396211, EBI-16059332; CC Q9UJX6; P50221: MEOX1; NbExp=3; IntAct=EBI-396211, EBI-2864512; CC Q9UJX6; Q16763: UBE2S; NbExp=4; IntAct=EBI-396211, EBI-2339823; CC Q9UJX6; P61964: WDR5; NbExp=3; IntAct=EBI-396211, EBI-540834; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UJX6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJX6-2; Sequence=VSP_008463; CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE- CC ProRule:PRU00330}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH09487.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={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; AF191337; AAF05751.1; -; mRNA. DR EMBL; AL929554; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032503; AAH32503.1; -; mRNA. DR EMBL; BC001579; AAH01579.1; -; mRNA. DR EMBL; BC009487; AAH09487.2; ALT_SEQ; mRNA. DR EMBL; AB037827; BAA92644.1; -; mRNA. DR CCDS; CCDS7033.1; -. [Q9UJX6-1] DR RefSeq; NP_037498.1; NM_013366.3. [Q9UJX6-1] DR PDB; 4UI9; EM; 3.60 A; N=1-822. DR PDB; 4YII; X-ray; 1.80 A; A=735-822. DR PDB; 5A31; EM; 4.30 A; N=74-818. DR PDB; 5G04; EM; 4.00 A; N=1-822. DR PDB; 5G05; EM; 3.40 A; N=1-822. DR PDB; 5KHR; EM; 6.10 A; N=1-822. DR PDB; 5KHU; EM; 4.80 A; N=1-822. DR PDB; 5L9T; EM; 6.40 A; N=1-822. DR PDB; 5L9U; EM; 6.40 A; N=1-822. DR PDB; 5LCW; EM; 4.00 A; N=1-822. DR PDB; 6NXK; X-ray; 2.20 A; C/D=735-822. DR PDB; 6OB1; NMR; -; C=735-822. DR PDB; 6Q6G; EM; 3.20 A; N=1-822. DR PDB; 6Q6H; EM; 3.20 A; N=1-822. DR PDB; 6TLJ; EM; 3.80 A; N=1-822. DR PDB; 6TM5; EM; 3.90 A; N=1-822. DR PDB; 6TNT; EM; 3.78 A; N=1-822. DR PDB; 7QE7; EM; 2.90 A; N=1-822. DR PDBsum; 4UI9; -. DR PDBsum; 4YII; -. 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; 6NXK; -. DR PDBsum; 6OB1; -. DR PDBsum; 6Q6G; -. DR PDBsum; 6Q6H; -. DR PDBsum; 6TLJ; -. DR PDBsum; 6TM5; -. DR PDBsum; 6TNT; -. DR PDBsum; 7QE7; -. DR AlphaFoldDB; Q9UJX6; -. DR SMR; Q9UJX6; -. DR BioGRID; 118937; 241. DR ComplexPortal; CPX-1860; Anaphase-promoting core complex. DR CORUM; Q9UJX6; -. DR DIP; DIP-32957N; -. DR IntAct; Q9UJX6; 43. DR MINT; Q9UJX6; -. DR STRING; 9606.ENSP00000314004; -. DR iPTMnet; Q9UJX6; -. DR PhosphoSitePlus; Q9UJX6; -. DR BioMuta; ANAPC2; -. DR DMDM; 37537863; -. DR EPD; Q9UJX6; -. DR jPOST; Q9UJX6; -. DR MassIVE; Q9UJX6; -. DR MaxQB; Q9UJX6; -. DR PaxDb; Q9UJX6; -. DR PeptideAtlas; Q9UJX6; -. DR ProteomicsDB; 84688; -. [Q9UJX6-1] DR ProteomicsDB; 84689; -. [Q9UJX6-2] DR TopDownProteomics; Q9UJX6-2; -. [Q9UJX6-2] DR ABCD; Q9UJX6; 3 sequenced antibodies. DR Antibodypedia; 4358; 335 antibodies from 32 providers. DR DNASU; 29882; -. DR Ensembl; ENST00000323927.3; ENSP00000314004.2; ENSG00000176248.9. [Q9UJX6-1] DR GeneID; 29882; -. DR KEGG; hsa:29882; -. DR MANE-Select; ENST00000323927.3; ENSP00000314004.2; NM_013366.4; NP_037498.1. DR UCSC; uc004clr.2; human. [Q9UJX6-1] DR AGR; HGNC:19989; -. DR CTD; 29882; -. DR DisGeNET; 29882; -. DR GeneCards; ANAPC2; -. DR HGNC; HGNC:19989; ANAPC2. DR HPA; ENSG00000176248; Low tissue specificity. DR MIM; 606946; gene. DR neXtProt; NX_Q9UJX6; -. DR OpenTargets; ENSG00000176248; -. DR PharmGKB; PA134884359; -. DR VEuPathDB; HostDB:ENSG00000176248; -. DR eggNOG; KOG2165; Eukaryota. DR GeneTree; ENSGT00390000016127; -. DR HOGENOM; CLU_007149_2_0_1; -. DR InParanoid; Q9UJX6; -. DR OMA; FMYETFA; -. DR OrthoDB; 2786196at2759; -. DR PhylomeDB; Q9UJX6; -. DR TreeFam; TF105442; -. DR PathwayCommons; Q9UJX6; -. 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; Q9UJX6; -. DR SIGNOR; Q9UJX6; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 29882; 804 hits in 1172 CRISPR screens. DR ChiTaRS; ANAPC2; human. DR GeneWiki; ANAPC2; -. DR GenomeRNAi; 29882; -. DR Pharos; Q9UJX6; Tbio. DR PRO; PR:Q9UJX6; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9UJX6; Protein. DR Bgee; ENSG00000176248; Expressed in right uterine tube and 163 other tissues. DR Genevisible; Q9UJX6; HS. DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro. DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; NAS:ComplexPortal. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl. DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:Ensembl. DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB. DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB. DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0051445; P:regulation of meiotic cell cycle; NAS:ComplexPortal. DR GO; GO:0007346; P:regulation of mitotic cell cycle; NAS:ComplexPortal. DR DisProt; DP01526; -. DR Gene3D; 1.20.1310.10; Cullin Repeats; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR044554; APC2-like. DR InterPro; IPR014786; APC2_C. DR InterPro; IPR016158; Cullin_homology. DR InterPro; IPR036317; Cullin_homology_sf. DR InterPro; IPR001373; Cullin_N. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR45957; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1. DR PANTHER; PTHR45957:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1. DR Pfam; PF08672; ANAPC2; 1. DR Pfam; PF00888; Cullin; 1. DR SMART; SM01013; APC2; 1. DR SMART; SM00182; CULLIN; 1. DR SUPFAM; SSF75632; Cullin homology domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50069; CULLIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; KW Differentiation; Mitosis; Neurogenesis; Phosphoprotein; Reference proteome; KW Ubl conjugation pathway. FT CHAIN 1..822 FT /note="Anaphase-promoting complex subunit 2" FT /id="PRO_0000119811" FT REGION 450..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 502..700 FT /note="Cullin homology" FT /evidence="ECO:0000269|PubMed:9469815" FT COMPBIAS 466..483 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 218 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:23186163" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:14657031, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163" FT MOD_RES 470 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 534 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:14657031, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 697 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BZQ7" FT MOD_RES 810 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q8BZQ7" FT VAR_SEQ 350..352 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008463" FT MUTAGEN 350 FT /note="D->K: Impairs UBE2S-mediated polyubiquitination, FT decreasing substrate affinity, does not affect UBE2C- FT mediated multiubiquitination; when associated with K-353." FT /evidence="ECO:0000269|PubMed:27259151" FT MUTAGEN 353 FT /note="D->K: Impairs UBE2S-mediated polyubiquitination, FT decreasing substrate affinity, does not affect UBE2C- FT mediated multiubiquitination; when associated with K-350." FT /evidence="ECO:0000269|PubMed:27259151" FT HELIX 18..31 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 52..64 FT /evidence="ECO:0007829|PDB:7QE7" FT TURN 65..70 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 71..85 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 87..99 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 104..138 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 149..162 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 167..188 FT /evidence="ECO:0007829|PDB:7QE7" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:7QE7" FT TURN 197..199 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 206..216 FT /evidence="ECO:0007829|PDB:7QE7" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 233..249 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 253..256 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 258..277 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 286..303 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 307..312 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 317..349 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 351..365 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 371..385 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 393..410 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 415..430 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 434..441 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 447..449 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 451..457 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 485..487 FT /evidence="ECO:0007829|PDB:6Q6G" FT HELIX 501..507 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 512..529 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 531..533 FT /evidence="ECO:0007829|PDB:6Q6G" FT HELIX 535..549 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 552..554 FT /evidence="ECO:0007829|PDB:6Q6H" FT HELIX 555..580 FT /evidence="ECO:0007829|PDB:7QE7" FT TURN 583..585 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 588..597 FT /evidence="ECO:0007829|PDB:7QE7" FT TURN 598..600 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 601..603 FT /evidence="ECO:0007829|PDB:6Q6G" FT HELIX 613..629 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 633..638 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 639..641 FT /evidence="ECO:0007829|PDB:6Q6G" FT STRAND 644..649 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 650..653 FT /evidence="ECO:0007829|PDB:6Q6G" FT STRAND 654..659 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 661..672 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 673..677 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 678..685 FT /evidence="ECO:0007829|PDB:7QE7" FT HELIX 689..700 FT /evidence="ECO:0007829|PDB:7QE7" FT TURN 701..703 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 704..709 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 712..715 FT /evidence="ECO:0007829|PDB:7QE7" FT STRAND 722..725 FT /evidence="ECO:0007829|PDB:6Q6G" FT HELIX 748..765 FT /evidence="ECO:0007829|PDB:4YII" FT HELIX 770..780 FT /evidence="ECO:0007829|PDB:4YII" FT TURN 781..783 FT /evidence="ECO:0007829|PDB:6NXK" FT HELIX 785..787 FT /evidence="ECO:0007829|PDB:6NXK" FT HELIX 792..804 FT /evidence="ECO:0007829|PDB:4YII" FT STRAND 807..811 FT /evidence="ECO:0007829|PDB:4YII" FT STRAND 814..816 FT /evidence="ECO:0007829|PDB:4YII" SQ SEQUENCE 822 AA; 93828 MW; 94A2B1D015805573 CRC64; MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISPE FWNAISQCEN SADEPQCLLL LLDAFGLLES RLDPYLRSLE LLEKWTRLGL LMGTGAQGLR EEVHTMLRGV LFFSTPRTFQ EMIQRLYGCF LRVYMQSKRK GEGGTDPELE GELDSRYARR RYYRLLQSPL CAGCSSDKQQ CWCRQALEQF HQLSQVLHRL SLLERVSAEA VTTTLHQVTR ERMEDRCRGE YERSFLREFH KWIERVVGWL GKVFLQDGPA RPASPEAGNT LRRWRCHVQR FFYRIYASLR IEELFSIVRD FPDSRPAIED LKYCLERTDQ RQQLLVSLKA ALETRLLHPG VNTCDIITLY ISAIKALRVL DPSMVILEVA CEPIRRYLRT REDTVRQIVA GLTGDSDGTG DLAVELSKTD PASLETGQDS EDDSGEPEDW VPDPVDADPG KSSSKRRSSD IISLLVSIYG SKDLFINEYR SLLADRLLHQ FSFSPEREIR NVELLKLRFG EAPMHFCEVM LKDMADSRRI NANIREEDEK RPAEEQPPFG VYAVILSSEF WPPFKDEKLE VPEDIRAALE AYCKKYEQLK AMRTLSWKHT LGLVTMDVEL ADRTLSVAVT PVQAVILLYF QDQASWTLEE LSKAVKMPVA LLRRRMSVWL QQGVLREEPP GTFSVIEEER PQDRDNMVLI DSDDESDSGM ASQADQKEEE LLLFWTYIQA MLTNLESLSL DRIYNMLRMF VVTGPALAEI DLQELQGYLQ KKVRDQQLVY SAGVYRLPKN CS //