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 16-OCT-2013, entry version 119. 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), AND 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; 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 MASS RP SPECTROMETRY. 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 MASS SPECTROMETRY. 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 MASS SPECTROMETRY. 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 MASS RP SPECTROMETRY. 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 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). CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls CC progression through mitosis and the G1 phase of the cell cycle. CC The APC/C complex acts by mediating ubiquitination and subsequent CC degradation of target proteins: it mainly mediates the formation CC of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, CC the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin CC chains. The CDC20-APC/C complex positively regulates the formation CC of synaptic vesicle clustering at active zone to the presynaptic CC membrane in postmitotic neurons. CDC20-APC/C-induced degradation CC of NEUROD2 drives presynaptic differentiation. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with NEUROD2 (By similarity). The APC/C is CC composed of at least 12 subunits. Interacts through the cullin CC domain with ANAPC11 and with UBCH10. 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. CC -!- SEQUENCE CAUTION: CC Sequence=AAH09487.2; Type=Erroneous translation; Note=Wrong choice of frame; 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; CAH72881.1; -; 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 IPI; IPI00002549; -. DR IPI; IPI00375832; -. DR RefSeq; NP_037498.1; NM_013366.3. DR UniGene; Hs.533262; -. DR ProteinModelPortal; Q9UJX6; -. DR SMR; Q9UJX6; 508-696. DR DIP; DIP-32957N; -. DR IntAct; Q9UJX6; 20. DR MINT; MINT-1196367; -. DR STRING; 9606.ENSP00000314004; -. DR PhosphoSite; Q9UJX6; -. DR DMDM; 37537863; -. DR PaxDb; Q9UJX6; -. DR PRIDE; Q9UJX6; -. DR DNASU; 29882; -. DR Ensembl; ENST00000323927; ENSP00000314004; ENSG00000176248. DR GeneID; 29882; -. DR KEGG; hsa:29882; -. DR UCSC; uc004clq.1; human. DR CTD; 29882; -. DR GeneCards; GC09M140069; -. DR HGNC; HGNC:19989; ANAPC2. DR HPA; CAB018692; -. DR MIM; 606946; gene. DR neXtProt; NX_Q9UJX6; -. DR PharmGKB; PA134884359; -. DR eggNOG; COG5647; -. DR HOGENOM; HOG000033936; -. DR HOVERGEN; HBG045327; -. DR InParanoid; Q9UJX6; -. DR KO; K03349; -. DR OMA; ELLVAWN; -. DR OrthoDB; EOG4T1HM4; -. DR PhylomeDB; Q9UJX6; -. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_21300; Mitotic M-M/G1 phases. DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; REACT_6900; Immune System. DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A. DR SignaLink; Q9UJX6; -. DR UniPathway; UPA00143; -. DR GeneWiki; ANAPC2; -. DR GenomeRNAi; 29882; -. DR NextBio; 52411; -. DR PRO; PR:Q9UJX6; -. DR ArrayExpress; Q9UJX6; -. DR Bgee; Q9UJX6; -. DR CleanEx; HS_ANAPC2; -. DR CleanEx; HS_APC2; -. DR Genevestigator; Q9UJX6; -. 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:0004842; F:ubiquitin-protein ligase activity; TAS:ProtInc. DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0008054; P:cyclin catabolic process; TAS:ProtInc. DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW. DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome. DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. 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:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014786; APC_su2_C. DR InterPro; IPR016158; Cullin_homology. DR InterPro; IPR001373; Cullin_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF08672; APC2; 1. DR Pfam; PF00888; Cullin; 1. DR SMART; SM01013; APC2; 1. DR SMART; SM00182; CULLIN; 1. DR SUPFAM; SSF75632; SSF75632; 1. DR PROSITE; PS01256; CULLIN_1; FALSE_NEG. DR PROSITE; PS50069; CULLIN_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cell division; Complete proteome; KW Differentiation; Mitosis; Neurogenesis; Phosphoprotein; KW Reference proteome; Ubl conjugation pathway. FT CHAIN 1 822 Anaphase-promoting complex subunit 2. FT /FTId=PRO_0000119811. FT MOD_RES 218 218 Phosphoserine. FT MOD_RES 314 314 Phosphoserine. FT MOD_RES 470 470 Phosphoserine. FT MOD_RES 534 534 Phosphoserine. FT MOD_RES 810 810 Phosphotyrosine (By similarity). FT VAR_SEQ 350 352 Missing (in isoform 2). FT /FTId=VSP_008463. 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 //