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 31-JUL-2019, entry version 177. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT anaphase-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., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA 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., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA 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., RA Rogers J., 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 RP SEQUENCE [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 RT project: 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. RT The complete sequences of 150 new cDNA clones from brain which code RT for large 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., RA Deisenhofer J., Yu H.; RT "APC2 cullin protein and APC11 RING protein comprise the minimal RT ubiquitin 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 RP BY 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 RT phosphorylation 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- RT promoting 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 RT the 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 RP SER-534, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION RP BY 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., RA Buerckstuemmer T., 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 RP SER-534, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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 RP 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 RT 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 RP 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 RP APC/C; UBE2C AND UBE2S, INTERACTION WITH UBE2C AND UBE2S, AND RP MUTAGENESIS OF 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., RA Stark H., 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 CC the catalytic component of the anaphase promoting CC complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin CC ligase that controls progression through mitosis and the G1 phase CC of the cell cycle. The APC/C complex acts by mediating CC ubiquitination and subsequent degradation of target proteins: it CC mainly mediates the formation of 'Lys-11'-linked polyubiquitin CC chains and, to a lower extent, the formation of 'Lys-48'- and CC 'Lys-63'-linked polyubiquitin chains. The CDC20-APC/C complex CC positively regulates the formation of synaptic vesicle clustering CC at active zone to the presynaptic membrane in postmitotic neurons. CC CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic CC 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, CC ANAPC15 and ANAPC16 that assemble into a complex of at least 19 CC chains with a combined molecular mass of around 1.2 MDa; APC/C CC interacts with FZR1 and FBXO5 (PubMed:25043029, PubMed:26083744). CC In the context of the APC/C complex, directly interacts with UBE2C CC and UBE2S (PubMed:27259151). Interacts (via cullin domain) with CC ANAPC11 and with UBCH10 (PubMed:11739784). Interacts with NEUROD2 CC (By similarity). {ECO:0000250|UniProtKB:Q8BZQ7, CC ECO:0000269|PubMed:11739784, ECO:0000269|PubMed:25043029, CC ECO:0000269|PubMed:26083744, ECO:0000269|PubMed:27259151}. CC -!- INTERACTION: CC Q9UKT4-1:FBXO5; NbExp=7; IntAct=EBI-396211, EBI-16059332; CC Q16763:UBE2S; NbExp=4; IntAct=EBI-396211, EBI-2339823; 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 Note=No experimental confirmation available.; 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 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 SMR; Q9UJX6; -. DR BioGrid; 118937; 65. DR CORUM; Q9UJX6; -. DR DIP; DIP-32957N; -. DR IntAct; Q9UJX6; 36. 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 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; -. 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 GeneCards; ANAPC2; -. DR HGNC; HGNC:19989; ANAPC2. DR HPA; CAB018692; -. DR HPA; HPA066539; -. 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; HOG000033936; -. DR InParanoid; Q9UJX6; -. DR KO; K03349; -. DR OMA; SMVVDIY; -. 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-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9UJX6; -. DR SIGNOR; Q9UJX6; -. DR UniPathway; UPA00143; -. DR ChiTaRS; ANAPC2; human. DR GeneWiki; ANAPC2; -. DR GenomeRNAi; 29882; -. DR PRO; PR:Q9UJX6; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; ENSG00000176248; Expressed in 193 organ(s), highest expression level in left lobe of thyroid gland. 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: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 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 Complete proteome; Differentiation; Mitosis; Neurogenesis; KW Phosphoprotein; Reference proteome; Ubl conjugation pathway. FT CHAIN 1 822 Anaphase-promoting complex subunit 2. FT /FTId=PRO_0000119811. FT REGION 502 700 Cullin homology. FT {ECO:0000269|PubMed:9469815}. FT MOD_RES 218 218 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 314 314 Phosphoserine. FT {ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:14657031}. FT MOD_RES 470 470 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332}. FT MOD_RES 534 534 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:14657031}. FT MOD_RES 697 697 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8BZQ7}. FT MOD_RES 810 810 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q8BZQ7}. FT VAR_SEQ 350 352 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_008463. FT MUTAGEN 350 350 D->K: Impairs UBE2S-mediated FT polyubiquitination, decreasing substrate FT affinity, does not affect UBE2C-mediated FT multiubiquitination; when associated with FT K-353. {ECO:0000269|PubMed:27259151}. FT MUTAGEN 353 353 D->K: Impairs UBE2S-mediated FT polyubiquitination, decreasing substrate FT affinity, does not affect UBE2C-mediated FT multiubiquitination; when associated with FT K-350. {ECO:0000269|PubMed:27259151}. FT HELIX 16 28 {ECO:0000244|PDB:5G05}. FT HELIX 52 65 {ECO:0000244|PDB:5G05}. FT HELIX 68 85 {ECO:0000244|PDB:5G05}. FT HELIX 87 99 {ECO:0000244|PDB:5G05}. FT HELIX 105 120 {ECO:0000244|PDB:5G05}. FT HELIX 123 137 {ECO:0000244|PDB:5G05}. FT STRAND 144 146 {ECO:0000244|PDB:5G05}. FT HELIX 148 161 {ECO:0000244|PDB:5G05}. FT STRAND 162 164 {ECO:0000244|PDB:5G05}. FT HELIX 167 190 {ECO:0000244|PDB:5G05}. FT HELIX 233 250 {ECO:0000244|PDB:5G05}. FT HELIX 254 277 {ECO:0000244|PDB:5G05}. FT HELIX 288 303 {ECO:0000244|PDB:5G05}. FT HELIX 322 342 {ECO:0000244|PDB:5G05}. FT HELIX 344 349 {ECO:0000244|PDB:5G05}. FT HELIX 355 367 {ECO:0000244|PDB:5G05}. FT HELIX 372 386 {ECO:0000244|PDB:5G05}. FT HELIX 393 408 {ECO:0000244|PDB:5G05}. FT HELIX 415 430 {ECO:0000244|PDB:5G05}. FT STRAND 431 434 {ECO:0000244|PDB:5G05}. FT HELIX 435 442 {ECO:0000244|PDB:5G05}. FT HELIX 500 509 {ECO:0000244|PDB:5G05}. FT HELIX 512 529 {ECO:0000244|PDB:5G05}. FT TURN 531 533 {ECO:0000244|PDB:5G05}. FT HELIX 535 548 {ECO:0000244|PDB:5G05}. FT HELIX 552 562 {ECO:0000244|PDB:5G05}. FT HELIX 565 579 {ECO:0000244|PDB:5G05}. FT HELIX 581 583 {ECO:0000244|PDB:5G05}. FT STRAND 598 600 {ECO:0000244|PDB:5G05}. FT HELIX 613 628 {ECO:0000244|PDB:5G05}. FT HELIX 639 641 {ECO:0000244|PDB:5G05}. FT STRAND 643 653 {ECO:0000244|PDB:5G05}. FT HELIX 661 671 {ECO:0000244|PDB:5G05}. FT STRAND 672 675 {ECO:0000244|PDB:5G05}. FT HELIX 678 685 {ECO:0000244|PDB:5G05}. FT HELIX 689 702 {ECO:0000244|PDB:5G05}. FT STRAND 709 711 {ECO:0000244|PDB:5G05}. FT STRAND 722 725 {ECO:0000244|PDB:5G05}. FT HELIX 748 765 {ECO:0000244|PDB:4YII}. FT HELIX 770 780 {ECO:0000244|PDB:4YII}. FT HELIX 792 804 {ECO:0000244|PDB:4YII}. FT STRAND 807 811 {ECO:0000244|PDB:4YII}. FT STRAND 814 816 {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 //