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Database: UniProt
Entry: Q9UJX6
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Original site: Q9UJX6 
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   17-JUN-2020, entry version 184.
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:0000244|PDB:4UI9, ECO:0000244|PDB:5A31}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF APC/C, AND SUBUNIT.
RX   PubMed=26083744; DOI=10.1038/nature14471;
RA   Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT   "Atomic structure of the APC/C and its mechanism of protein
RT   ubiquitination.";
RL   Nature 522:450-454(2015).
RN   [20] {ECO:0000244|PDB:5L9T, ECO:0000244|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};
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   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   SMR; Q9UJX6; -.
DR   BioGRID; 118937; 69.
DR   CORUM; Q9UJX6; -.
DR   DIP; DIP-32957N; -.
DR   IntAct; Q9UJX6; 41.
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   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; 270 antibodies.
DR   DNASU; 29882; -.
DR   Ensembl; ENST00000323927; ENSP00000314004; ENSG00000176248. [Q9UJX6-1]
DR   GeneID; 29882; -.
DR   KEGG; hsa:29882; -.
DR   UCSC; uc004clr.2; human. [Q9UJX6-1]
DR   CTD; 29882; -.
DR   EuPathDB; HostDB:ENSG00000176248.8; -.
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   eggNOG; KOG2165; Eukaryota.
DR   eggNOG; ENOG410XRBY; LUCA.
DR   GeneTree; ENSGT00390000016127; -.
DR   HOGENOM; CLU_007149_2_0_1; -.
DR   InParanoid; Q9UJX6; -.
DR   KO; K03349; -.
DR   OMA; VNTMDIL; -.
DR   OrthoDB; 570797at2759; -.
DR   PhylomeDB; Q9UJX6; -.
DR   TreeFam; TF105442; -.
DR   Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR   Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q9UJX6; -.
DR   SIGNOR; Q9UJX6; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 29882; 708 hits in 793 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 left lobe of thyroid gland and 192 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; TAS:Reactome.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
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:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   DisProt; DP01526; -.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR014786; APC_su2_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   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          502..700
FT                   /note="Cullin homology"
FT                   /evidence="ECO:0000269|PubMed:9469815"
FT   MOD_RES         218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031"
FT   MOD_RES         470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332"
FT   MOD_RES         534
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031"
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..29
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           54..64
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            65..69
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   HELIX           70..85
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           87..100
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           104..137
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          138..141
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          145..147
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           149..161
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          162..164
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           167..189
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           190..192
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          193..195
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           206..214
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           215..217
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   HELIX           235..249
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           253..256
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           258..277
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           286..303
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           315..342
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           344..349
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            350..353
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           356..365
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           371..385
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           393..410
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           416..420
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           422..429
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          431..433
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   HELIX           434..440
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            441..443
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          446..450
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           451..455
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          485..487
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           501..505
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           506..508
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           513..527
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          531..533
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           537..549
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           552..556
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           558..565
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            566..568
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           569..573
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            574..576
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          578..580
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           581..583
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          588..591
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   STRAND          598..600
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          601..603
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           615..629
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          639..641
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          650..653
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           661..668
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          669..672
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           678..684
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           689..692
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            696..698
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           699..702
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          709..711
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          722..725
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           748..765
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   HELIX           770..780
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   TURN            781..783
FT                   /evidence="ECO:0000244|PDB:6NXK"
FT   HELIX           785..787
FT                   /evidence="ECO:0000244|PDB:6NXK"
FT   HELIX           792..804
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   STRAND          807..811
FT                   /evidence="ECO:0000244|PDB:4YII"
FT   STRAND          814..816
FT                   /evidence="ECO:0000244|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
//
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