APC5_HUMAN
ID APC5_HUMAN Reviewed; 755 AA.
AC Q9UJX4; E9PFB2; Q8N4H7; Q9BQD4;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Anaphase-promoting complex subunit 5;
DE Short=APC5;
DE AltName: Full=Cyclosome subunit 5;
GN Name=ANAPC5; Synonyms=APC5;
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), 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 anaphase-
RT promoting complex.";
RL Science 279:1219-1222(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Esophagus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Cervix, and Lung;
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 [6]
RP PHOSPHORYLATION AT SER-195.
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 [7]
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [9]
RP IDENTIFICATION 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 [10]
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 [11]
RP TPR REPEATS.
RX PubMed=21307936; DOI=10.1038/nature09756;
RA Schreiber A., Stengel F., Zhang Z., Enchev R.I., Kong E.H., Morris E.P.,
RA Robinson C.V., da Fonseca P.C., Barford D.;
RT "Structural basis for the subunit assembly of the anaphase-promoting
RT complex.";
RL Nature 470:227-232(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
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 [14]
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 [15] {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 [16]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-617.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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. 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.
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. {ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744,
CC ECO:0000269|PubMed:9469815}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:18445686}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UJX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJX4-2; Sequence=VSP_008466, VSP_008467, VSP_008468,
CC VSP_008469;
CC Name=3;
CC IsoId=Q9UJX4-3; Sequence=VSP_044878, VSP_044879;
CC -!- DOMAIN: The TPR repeats are six to seven residues longer than a
CC canonical TPR motif. {ECO:0000269|PubMed:21307936}.
CC -!- SIMILARITY: Belongs to the APC5 family. {ECO:0000305}.
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DR EMBL; AF191339; AAF05753.1; -; mRNA.
DR EMBL; AK025614; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX537687; CAD97812.1; -; mRNA.
DR EMBL; AC048337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001081; AAH01081.1; -; mRNA.
DR EMBL; BC001950; AAH01950.1; -; mRNA.
DR EMBL; BC006301; AAH06301.1; -; mRNA.
DR EMBL; BC034243; AAH34243.1; -; mRNA.
DR CCDS; CCDS45000.1; -. [Q9UJX4-3]
DR CCDS; CCDS9220.1; -. [Q9UJX4-1]
DR RefSeq; NP_001131031.1; NM_001137559.1. [Q9UJX4-3]
DR RefSeq; NP_001317418.1; NM_001330489.1.
DR RefSeq; NP_057321.2; NM_016237.4. [Q9UJX4-1]
DR PDB; 4UI9; EM; 3.60 A; O=1-755.
DR PDB; 5A31; EM; 4.30 A; O=1-755.
DR PDB; 5G04; EM; 4.00 A; O=1-755.
DR PDB; 5G05; EM; 3.40 A; O=1-755.
DR PDB; 5KHR; EM; 6.10 A; O=1-755.
DR PDB; 5KHU; EM; 4.80 A; O=1-755.
DR PDB; 5L9T; EM; 6.40 A; O=1-755.
DR PDB; 5L9U; EM; 6.40 A; O=1-755.
DR PDB; 5LCW; EM; 4.00 A; O=1-755.
DR PDB; 6Q6G; EM; 3.20 A; O=1-755.
DR PDB; 6Q6H; EM; 3.20 A; O=1-755.
DR PDB; 6TLJ; EM; 3.80 A; O=1-755.
DR PDB; 6TM5; EM; 3.90 A; O=1-755.
DR PDB; 6TNT; EM; 3.78 A; O=1-755.
DR PDB; 7QE7; EM; 2.90 A; O=1-755.
DR PDBsum; 4UI9; -.
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; 6Q6G; -.
DR PDBsum; 6Q6H; -.
DR PDBsum; 6TLJ; -.
DR PDBsum; 6TM5; -.
DR PDBsum; 6TNT; -.
DR PDBsum; 7QE7; -.
DR AlphaFoldDB; Q9UJX4; -.
DR SMR; Q9UJX4; -.
DR BioGRID; 119537; 152.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR CORUM; Q9UJX4; -.
DR DIP; DIP-32945N; -.
DR IntAct; Q9UJX4; 61.
DR MINT; Q9UJX4; -.
DR STRING; 9606.ENSP00000261819; -.
DR iPTMnet; Q9UJX4; -.
DR MetOSite; Q9UJX4; -.
DR PhosphoSitePlus; Q9UJX4; -.
DR SwissPalm; Q9UJX4; -.
DR BioMuta; ANAPC5; -.
DR DMDM; 37537861; -.
DR EPD; Q9UJX4; -.
DR jPOST; Q9UJX4; -.
DR MassIVE; Q9UJX4; -.
DR MaxQB; Q9UJX4; -.
DR PaxDb; Q9UJX4; -.
DR PeptideAtlas; Q9UJX4; -.
DR PRIDE; Q9UJX4; -.
DR ProteomicsDB; 20064; -.
DR ProteomicsDB; 84684; -. [Q9UJX4-1]
DR ProteomicsDB; 84685; -. [Q9UJX4-2]
DR Antibodypedia; 31562; 374 antibodies from 37 providers.
DR DNASU; 51433; -.
DR Ensembl; ENST00000261819.8; ENSP00000261819.3; ENSG00000089053.13. [Q9UJX4-1]
DR Ensembl; ENST00000441917.6; ENSP00000415061.2; ENSG00000089053.13. [Q9UJX4-3]
DR GeneID; 51433; -.
DR KEGG; hsa:51433; -.
DR MANE-Select; ENST00000261819.8; ENSP00000261819.3; NM_016237.5; NP_057321.2.
DR UCSC; uc001uag.4; human. [Q9UJX4-1]
DR CTD; 51433; -.
DR DisGeNET; 51433; -.
DR GeneCards; ANAPC5; -.
DR HGNC; HGNC:15713; ANAPC5.
DR HPA; ENSG00000089053; Low tissue specificity.
DR MIM; 606948; gene.
DR neXtProt; NX_Q9UJX4; -.
DR OpenTargets; ENSG00000089053; -.
DR PharmGKB; PA24788; -.
DR VEuPathDB; HostDB:ENSG00000089053; -.
DR eggNOG; KOG4322; Eukaryota.
DR GeneTree; ENSGT00390000018674; -.
DR HOGENOM; CLU_020635_0_0_1; -.
DR InParanoid; Q9UJX4; -.
DR OMA; TVMHLTG; -.
DR OrthoDB; 240631at2759; -.
DR PhylomeDB; Q9UJX4; -.
DR TreeFam; TF105444; -.
DR PathwayCommons; Q9UJX4; -.
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; Q9UJX4; -.
DR SIGNOR; Q9UJX4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 51433; 741 hits in 1096 CRISPR screens.
DR ChiTaRS; ANAPC5; human.
DR GeneWiki; ANAPC5; -.
DR GenomeRNAi; 51433; -.
DR Pharos; Q9UJX4; Tbio.
DR PRO; PR:Q9UJX4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UJX4; protein.
DR Bgee; ENSG00000089053; Expressed in right uterine tube and 213 other tissues.
DR ExpressionAtlas; Q9UJX4; baseline and differential.
DR Genevisible; Q9UJX4; 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:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
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; DP01443; -.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR037679; Apc5.
DR InterPro; IPR026000; Apc5_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12830; PTHR12830; 1.
DR Pfam; PF12862; ANAPC5; 2.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..755
FT /note="Anaphase-promoting complex subunit 5"
FT /id="PRO_0000064597"
FT REPEAT 209..249
FT /note="TPR 1"
FT REPEAT 250..300
FT /note="TPR 2"
FT REPEAT 301..337
FT /note="TPR 3"
FT REPEAT 338..378
FT /note="TPR 4"
FT REPEAT 379..418
FT /note="TPR 5"
FT REPEAT 419..466
FT /note="TPR 6"
FT REPEAT 467..500
FT /note="TPR 7"
FT REPEAT 501..540
FT /note="TPR 8"
FT REPEAT 541..580
FT /note="TPR 9"
FT REPEAT 581..620
FT /note="TPR 10"
FT REPEAT 621..660
FT /note="TPR 11"
FT REPEAT 661..696
FT /note="TPR 12"
FT REPEAT 697..736
FT /note="TPR 13"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008466"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044878"
FT VAR_SEQ 122..131
FT /note="TEPEVHKTSV -> MLSPCLSSYF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008467"
FT VAR_SEQ 318..340
FT /note="QQAELALQEAIRIAQESNDHVCL -> TSPPWEYSPLFNRELLLGRRQTS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008468"
FT VAR_SEQ 341..755
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008469"
FT VAR_SEQ 375..387
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044879"
FT VARIANT 617
FT /note="Q -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035793"
FT CONFLICT 24
FT /note="F -> L (in Ref. 1; AAF05753)"
FT /evidence="ECO:0000305"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 87..102
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 148..169
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 209..225
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 299..314
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 317..333
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 374..391
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 415..431
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 435..446
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 465..478
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 483..496
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 504..520
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 525..538
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 540..553
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 557..573
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 577..590
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 591..593
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 600..613
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 617..633
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 637..647
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 649..653
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 657..674
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 680..703
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 707..724
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 727..741
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 750..752
FT /evidence="ECO:0007829|PDB:7QE7"
SQ SEQUENCE 755 AA; 85077 MW; 174F68EAB44760EB CRC64;
MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL
NQLLLPLLQG PDITLSKLYK LIEESCPQLA NSVQIRIKLM AEGELKDMEQ FFDDLSDSFS
GTEPEVHKTS VVGLFLRHMI LAYSKLSFSQ VFKLYTALQQ YFQNGEKKTV EDADMELTSR
DEGERKMEKE ELDVSVREEE VSCSGPLSQK QAEFFLSQQA SLLKNDETKA LTPASLQKEL
NNLLKFNPDF AEAHYLSYLN NLRVQDVFSS THSLLHYFDR LILTGAESKS NGEEGYGRSL
RYAALNLAAL HCRFGHYQQA ELALQEAIRI AQESNDHVCL QHCLSWLYVL GQKRSDSYVL
LEHSVKKAVH FGLPYLASLG IQSLVQQRAF AGKTANKLMD ALKDSDLLHW KHSLSELIDI
SIAQKTAIWR LYGRSTMALQ QAQMLLSMNS LEAVNAGVQQ NNTESFAVAL CHLAELHAEQ
GCFAAASEVL KHLKERFPPN SQHAQLWMLC DQKIQFDRAM NDGKYHLADS LVTGITALNS
IEGVYRKAVV LQAQNQMSEA HKLLQKLLVH CQKLKNTEMV ISVLLSVAEL YWRSSSPTIA
LPMLLQALAL SKEYRLQYLA SETVLNLAFA QLILGIPEQA LSLLHMAIEP ILADGAILDK
GRAMFLVAKC QVASAASYDQ PKKAEALEAA IENLNEAKNY FAKVDCKERI RDVVYFQARL
YHTLGKTQER NRCAMLFRQL HQELPSHGVP LINHL
