ANC2_HUMAN
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 03-AUG-2022, entry version 194.
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).
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 {ECO:0000250|UniProtKB:Q8BZQ7, ECO:0000269|PubMed:11739784,
CC ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744,
CC ECO:0000269|PubMed:27259151}.
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};
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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; 228.
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 PRIDE; 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; 301 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 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; 570797at2759; -.
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; 767 hits in 1095 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; IC: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; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR DisProt; DP01526; -.
DR Gene3D; 1.10.10.10; -; 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; PTHR45957; 1.
DR Pfam; PF08672; ANAPC2; 1.
DR Pfam; PF00888; Cullin; 1.
DR SMART; SM01013; APC2; 1.
DR SMART; SM00182; CULLIN; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF75632; SSF75632; 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
