GenomeNet

Database: UniProt
Entry: Q9UJX5
LinkDB: Q9UJX5
Original site: Q9UJX5 
ID   APC4_HUMAN              Reviewed;         808 AA.
AC   Q9UJX5; A8K8H1; E9PCR4; Q6PCC6; Q9NSH6;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   17-JUN-2020, entry version 171.
DE   RecName: Full=Anaphase-promoting complex subunit 4;
DE            Short=APC4;
DE   AltName: Full=Cyclosome subunit 4;
GN   Name=ANAPC4; Synonyms=APC4;
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 1).
RC   TISSUE=Testis;
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 GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-808 (ISOFORM 2).
RC   TISSUE=Amygdala;
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   [6]
RP   PHOSPHORYLATION AT TYR-469 AND SER-779.
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=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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757; SER-758 AND SER-777, AND
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].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777, AND IDENTIFICATION BY
RP   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   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-772 AND LYS-798, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
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: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   [16] {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 UBE2S, AND MUTAGENESIS OF ASP-33.
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).
RN   [17]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-155.
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 (PubMed:25043029, PubMed:27259151, PubMed:9469815,
CC       PubMed:26083744). In the context of the APC/C complex, directly
CC       interacts with UBE2S (PubMed:27259151). {ECO:0000269|PubMed:25043029,
CC       ECO:0000269|PubMed:26083744, ECO:0000269|PubMed:27259151,
CC       ECO:0000269|PubMed:9469815}.
CC   -!- INTERACTION:
CC       Q9UJX5; Q12834: CDC20; NbExp=9; IntAct=EBI-2554854, EBI-367462;
CC       Q9UJX5; P30260: CDC27; NbExp=8; IntAct=EBI-2554854, EBI-994813;
CC       Q9UJX5; Q8NI77: KIF18A; NbExp=2; IntAct=EBI-2554854, EBI-355426;
CC       Q9UJX5; P51955: NEK2; NbExp=6; IntAct=EBI-2554854, EBI-633182;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UJX5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UJX5-2; Sequence=VSP_008464, VSP_008465;
CC       Name=3;
CC         IsoId=Q9UJX5-3; Sequence=VSP_056708;
CC   -!- SIMILARITY: Belongs to the APC4 family. {ECO:0000305}.
DR   EMBL; AF191338; AAF05752.1; -; mRNA.
DR   EMBL; AK292336; BAF85025.1; -; mRNA.
DR   EMBL; CH471069; EAW92839.1; -; Genomic_DNA.
DR   EMBL; BC059383; AAH59383.1; -; mRNA.
DR   EMBL; AL353932; CAB89245.1; -; mRNA.
DR   CCDS; CCDS3434.1; -. [Q9UJX5-1]
DR   CCDS; CCDS68684.1; -. [Q9UJX5-3]
DR   PIR; T48682; T48682.
DR   RefSeq; NP_001273685.1; NM_001286756.1. [Q9UJX5-3]
DR   RefSeq; NP_037499.2; NM_013367.2. [Q9UJX5-1]
DR   PDB; 4UI9; EM; 3.60 A; I=1-808.
DR   PDB; 5A31; EM; 4.30 A; I=1-808.
DR   PDB; 5BPW; X-ray; 3.40 A; A=1-808.
DR   PDB; 5G04; EM; 4.00 A; I=1-808.
DR   PDB; 5G05; EM; 3.40 A; I=1-808.
DR   PDB; 5KHR; EM; 6.10 A; I=1-808.
DR   PDB; 5KHU; EM; 4.80 A; I=1-808.
DR   PDB; 5L9T; EM; 6.40 A; I=1-808.
DR   PDB; 5L9U; EM; 6.40 A; I=1-808.
DR   PDB; 5LCW; EM; 4.00 A; I=1-808.
DR   PDB; 6Q6G; EM; 3.20 A; I=1-808.
DR   PDB; 6Q6H; EM; 3.20 A; I=1-808.
DR   PDB; 6TLJ; EM; 3.80 A; I=1-808.
DR   PDB; 6TM5; EM; 3.90 A; I=1-808.
DR   PDBsum; 4UI9; -.
DR   PDBsum; 5A31; -.
DR   PDBsum; 5BPW; -.
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; Q9UJX5; -.
DR   BioGRID; 118982; 103.
DR   CORUM; Q9UJX5; -.
DR   DIP; DIP-56450N; -.
DR   IntAct; Q9UJX5; 48.
DR   MINT; Q9UJX5; -.
DR   STRING; 9606.ENSP00000426654; -.
DR   iPTMnet; Q9UJX5; -.
DR   PhosphoSitePlus; Q9UJX5; -.
DR   BioMuta; ANAPC4; -.
DR   DMDM; 205371737; -.
DR   EPD; Q9UJX5; -.
DR   jPOST; Q9UJX5; -.
DR   MassIVE; Q9UJX5; -.
DR   PaxDb; Q9UJX5; -.
DR   PeptideAtlas; Q9UJX5; -.
DR   PRIDE; Q9UJX5; -.
DR   ProteomicsDB; 19498; -.
DR   ProteomicsDB; 84686; -. [Q9UJX5-1]
DR   ProteomicsDB; 84687; -. [Q9UJX5-2]
DR   Antibodypedia; 23215; 202 antibodies.
DR   Ensembl; ENST00000315368; ENSP00000318775; ENSG00000053900. [Q9UJX5-1]
DR   Ensembl; ENST00000510092; ENSP00000426654; ENSG00000053900. [Q9UJX5-3]
DR   GeneID; 29945; -.
DR   KEGG; hsa:29945; -.
DR   UCSC; uc003gro.4; human. [Q9UJX5-1]
DR   CTD; 29945; -.
DR   DisGeNET; 29945; -.
DR   EuPathDB; HostDB:ENSG00000053900.10; -.
DR   GeneCards; ANAPC4; -.
DR   HGNC; HGNC:19990; ANAPC4.
DR   HPA; ENSG00000053900; Low tissue specificity.
DR   MIM; 606947; gene.
DR   neXtProt; NX_Q9UJX5; -.
DR   OpenTargets; ENSG00000053900; -.
DR   PharmGKB; PA134894250; -.
DR   eggNOG; KOG4640; Eukaryota.
DR   eggNOG; ENOG410XPXK; LUCA.
DR   GeneTree; ENSGT00390000004612; -.
DR   HOGENOM; CLU_018724_0_0_1; -.
DR   InParanoid; Q9UJX5; -.
DR   KO; K03351; -.
DR   OMA; MRACGAF; -.
DR   PhylomeDB; Q9UJX5; -.
DR   TreeFam; TF105443; -.
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; Q9UJX5; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 29945; 733 hits in 792 CRISPR screens.
DR   ChiTaRS; ANAPC4; human.
DR   GeneWiki; ANAPC4; -.
DR   GenomeRNAi; 29945; -.
DR   Pharos; Q9UJX5; Tbio.
DR   PRO; PR:Q9UJX5; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9UJX5; protein.
DR   Bgee; ENSG00000053900; Expressed in endometrium and 205 other tissues.
DR   ExpressionAtlas; Q9UJX5; baseline and differential.
DR   Genevisible; Q9UJX5; HS.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0034399; C:nuclear periphery; IBA:GO_Central.
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:0004842; F:ubiquitin-protein transferase activity; TAS:ProtInc.
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; DP01478; -.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR024789; APC4.
DR   InterPro; IPR024790; APC4_long_dom.
DR   InterPro; IPR017169; APC4_metazoa.
DR   InterPro; IPR024977; Apc4_WD40_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13260; PTHR13260; 1.
DR   Pfam; PF12896; ANAPC4; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   PIRSF; PIRSF037303; APC4; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; Cell division;
KW   Isopeptide bond; Mitosis; Phosphoprotein; Polymorphism; Reference proteome;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..808
FT                   /note="Anaphase-promoting complex subunit 4"
FT                   /id="PRO_0000064595"
FT   MOD_RES         469
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   MOD_RES         757
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         758
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         777
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         779
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   CROSSLNK        772
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        798
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         439
FT                   /note="K -> KV (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_056708"
FT   VAR_SEQ         542..551
FT                   /note="DVIGKSMNQA -> VSLKEMHVFV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_008464"
FT   VAR_SEQ         552..808
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_008465"
FT   VARIANT         155
FT                   /note="I -> V (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035792"
FT   VARIANT         465
FT                   /note="R -> Q (in dbSNP:rs34811474)"
FT                   /id="VAR_054044"
FT   VARIANT         800
FT                   /note="E -> G (in dbSNP:rs11550697)"
FT                   /id="VAR_054045"
FT   MUTAGEN         33
FT                   /note="D->K: Impairs UBE2S-mediated polyubiquitination,
FT                   decreasing substrate affinity. Does not affect UBE2C-
FT                   mediated multiubiquitination."
FT                   /evidence="ECO:0000269|PubMed:27259151"
FT   CONFLICT        286
FT                   /note="R -> C (in Ref. 1; AAF05752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293..295
FT                   /note="EKN -> GKD (in Ref. 1; AAF05752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        756
FT                   /note="E -> G (in Ref. 4; AAH59383)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..15
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          23..28
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          30..33
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          35..39
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          44..47
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          49..52
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          54..58
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            62..64
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          68..73
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          79..84
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            85..88
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          89..99
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          101..105
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          114..117
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           120..122
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           133..136
FT                   /evidence="ECO:0000244|PDB:5BPW"
FT   STRAND          156..160
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           162..164
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            165..168
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          169..171
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          174..177
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          181..183
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          185..189
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            190..192
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          193..198
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          203..210
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          214..224
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          229..237
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           239..243
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           245..274
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            277..281
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           282..288
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           290..293
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           300..309
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          310..312
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           315..323
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           329..348
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            349..351
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           352..371
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            373..375
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            377..380
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           383..426
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            427..429
FT                   /evidence="ECO:0000244|PDB:5BPW"
FT   HELIX           442..455
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           476..479
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           496..502
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           507..509
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          511..513
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          518..520
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           522..546
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          553..560
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           561..563
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          573..578
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            579..582
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          583..592
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          595..608
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          615..623
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          626..628
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   STRAND          638..654
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            659..661
FT                   /evidence="ECO:0000244|PDB:5BPW"
FT   STRAND          664..670
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            671..675
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           677..680
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            693..699
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          702..707
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          709..713
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          719..724
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          726..735
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          740..748
FT                   /evidence="ECO:0000244|PDB:6Q6G"
SQ   SEQUENCE   808 AA;  92116 MW;  80362CC8D8B2063F CRC64;
     MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA SFHRVWSFPP
     NENTGKEVTC LAWRPDGKLL AFALADTKKI VLCDVEKPES LHSFSVEAPV SCMHWMEVTV
     ESSVLTSFYN AEDESNLLLP KLPTLPKNYS NTSKIFSEEN SDEIIKLLGD VRLNILVLGG
     SSGFIELYAY GMFKIARVTG IAGTCLALCL SSDLKSLSVV TEVSTNGASE VSYFQLETNL
     LYSFLPEVTR MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKNTTTSV
     QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS HLQSGSESLL
     YHLSELKGMA SWKQKYEPLG LDAAGIEEAI TAVGSFILKA NELLQVIDSS MKNFKAFFRW
     LYVAMLRMTE DHVLPELNKM TQKDITFVAE FLTEHFNEAP DLYNRKGKYF NVERVGQYLK
     DEDDDLVSPP NTEGNQWYDF LQNSSHLKES PLLFPYYPRK SLHFVKRRME NIIDQCLQKP
     ADVIGKSMNQ AICIPLYRDT RSEDSTRRLF KFPFLWNNKT SNLHYLLFTI LEDSLYKMCI
     LRRHTDISQS VSNGLIAIKF GSFTYATTEK VRRSIYSCLD AQFYDDETVT VVLKDTVGRE
     GRDRLLVQLP LSLVYNSEDS AEYQFTGTYS TRLDEQCSAI PTRTMHFEKH WRLLESMKAQ
     YVAGNGFRKV SCVLSSNLRH VRVFEMDIDD EWELDESSDE EEEASNKPVK IKEEVLSESE
     AENQQAGAAA LAPEIVIKVE KLDPELDS
//
DBGET integrated database retrieval system