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Database: UniProt
Entry: Q9UJX4
LinkDB: Q9UJX4
Original site: Q9UJX4 
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   17-JUN-2020, entry version 181.
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   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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [14] {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   [15]
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   -!- 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}.
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   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   SMR; Q9UJX4; -.
DR   BioGRID; 119537; 88.
DR   CORUM; Q9UJX4; -.
DR   DIP; DIP-32945N; -.
DR   IntAct; Q9UJX4; 57.
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   PaxDb; Q9UJX4; -.
DR   PeptideAtlas; Q9UJX4; -.
DR   PRIDE; Q9UJX4; -.
DR   ProteomicsDB; 20064; -.
DR   ProteomicsDB; 84684; -. [Q9UJX4-1]
DR   ProteomicsDB; 84685; -. [Q9UJX4-2]
DR   Antibodypedia; 31562; 339 antibodies.
DR   Ensembl; ENST00000261819; ENSP00000261819; ENSG00000089053. [Q9UJX4-1]
DR   Ensembl; ENST00000441917; ENSP00000415061; ENSG00000089053. [Q9UJX4-3]
DR   GeneID; 51433; -.
DR   KEGG; hsa:51433; -.
DR   UCSC; uc001uag.4; human. [Q9UJX4-1]
DR   CTD; 51433; -.
DR   DisGeNET; 51433; -.
DR   EuPathDB; HostDB:ENSG00000089053.12; -.
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   eggNOG; KOG4322; Eukaryota.
DR   eggNOG; ENOG410YVZN; LUCA.
DR   GeneTree; ENSGT00390000018674; -.
DR   HOGENOM; CLU_020635_0_0_1; -.
DR   InParanoid; Q9UJX4; -.
DR   KO; K03352; -.
DR   OMA; FSTCYKY; -.
DR   OrthoDB; 240631at2759; -.
DR   PhylomeDB; Q9UJX4; -.
DR   TreeFam; TF105444; -.
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   SIGNOR; Q9UJX4; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 51433; 697 hits in 789 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 body of pancreas and 235 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:BHF-UCL.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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: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; 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; Mitosis;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; TPR repeat;
KW   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:0000244|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   HELIX           32..44
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          47..49
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           54..69
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           75..85
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           87..102
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           105..115
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           116..119
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          128..130
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           131..144
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           148..166
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           209..225
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            227..229
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           233..246
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           252..262
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            263..265
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           268..280
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          287..289
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   HELIX           299..313
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           317..333
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           338..350
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            351..353
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          354..356
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           357..369
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          370..372
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           374..389
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            390..392
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           395..411
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           416..431
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           435..447
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           464..479
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           483..496
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           504..520
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            521..523
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           525..538
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           540..552
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            553..555
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           557..574
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           577..591
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           597..600
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           601..612
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            613..615
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           617..633
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           637..644
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           649..653
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           657..674
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           675..677
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           680..704
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           707..724
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           727..741
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            750..752
FT                   /evidence="ECO:0000244|PDB:6Q6G"
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
//
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