APC4_HUMAN
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 03-AUG-2022, entry version 181.
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 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=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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16] {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 [17] {ECO:0007744|PDB:5L9T, ECO:0007744|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 [18]
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686}.
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}.
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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 PDB; 6TNT; EM; 3.78 A; I=1-808.
DR PDB; 7QE7; EM; 2.90 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 PDBsum; 6TNT; -.
DR PDBsum; 7QE7; -.
DR AlphaFoldDB; Q9UJX5; -.
DR SMR; Q9UJX5; -.
DR BioGRID; 118982; 121.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR CORUM; Q9UJX5; -.
DR DIP; DIP-56450N; -.
DR IntAct; Q9UJX5; 52.
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 MaxQB; 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; 217 antibodies from 34 providers.
DR DNASU; 29945; -.
DR Ensembl; ENST00000315368.8; ENSP00000318775.3; ENSG00000053900.11. [Q9UJX5-1]
DR Ensembl; ENST00000510092.5; ENSP00000426654.1; ENSG00000053900.11. [Q9UJX5-3]
DR GeneID; 29945; -.
DR KEGG; hsa:29945; -.
DR MANE-Select; ENST00000315368.8; ENSP00000318775.3; NM_013367.3; NP_037499.2.
DR UCSC; uc003gro.4; human. [Q9UJX5-1]
DR CTD; 29945; -.
DR DisGeNET; 29945; -.
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 VEuPathDB; HostDB:ENSG00000053900; -.
DR eggNOG; KOG4640; Eukaryota.
DR GeneTree; ENSGT00390000004612; -.
DR HOGENOM; CLU_018724_0_0_1; -.
DR InParanoid; Q9UJX5; -.
DR OMA; HCKLFVP; -.
DR PhylomeDB; Q9UJX5; -.
DR TreeFam; TF105443; -.
DR PathwayCommons; Q9UJX5; -.
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; Q9UJX5; -.
DR SIGNOR; Q9UJX5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 29945; 788 hits in 1064 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 oviduct epithelium and 185 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:UniProtKB.
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: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 GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
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; Nucleus; Phosphoprotein; 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:0007744|PubMed:19690332"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|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:0007744|PubMed:28112733"
FT CROSSLNK 798
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|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..18
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:5BPW"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 214..225
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 245..275
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 327..370
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 383..427
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 443..455
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 496..503
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 522..547
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 549..559
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 573..578
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 583..592
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 595..606
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 615..623
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 626..628
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 636..642
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 644..658
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 660..665
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 671..674
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 678..682
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 697..699
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 702..710
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 713..717
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 719..725
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 726..729
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 730..735
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 740..748
FT /evidence="ECO:0007829|PDB:7QE7"
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
