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Database: UniProt
Entry: Q9BS18
LinkDB: Q9BS18
Original site: Q9BS18 
ID   APC13_HUMAN             Reviewed;          74 AA.
AC   Q9BS18; Q9Y3V0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   17-JUN-2020, entry version 134.
DE   RecName: Full=Anaphase-promoting complex subunit 13;
DE            Short=APC13;
DE   AltName: Full=Cyclosome subunit 13;
GN   Name=ANAPC13;
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 [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [3]
RP   FUNCTION.
RX   PubMed=15060174; DOI=10.1128/mcb.24.8.3562-3576.2004;
RA   Schwickart M., Havlis J., Habermann B., Bogdanova A., Camasses A.,
RA   Oelschlaegel T., Shevchenko A., Zachariae W.;
RT   "Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-
RT   promoting complex stabilizing the association of Cdc16 and Cdc27.";
RL   Mol. Cell. Biol. 24:3562-3576(2004).
RN   [4]
RP   IDENTIFICATION IN THE APC/C COMPLEX.
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   [5]
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   [6]
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   [7] {ECO:0000244|PDB:4UI9}
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).
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:15060174, 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:16364912, ECO:0000269|PubMed:25043029,
CC       ECO:0000269|PubMed:26083744}.
CC   -!- INTERACTION:
CC       Q9BS18; Q9UJX2: CDC23; NbExp=7; IntAct=EBI-2555953, EBI-396137;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the APC13 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB43251.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
DR   EMBL; AL050051; CAB43251.1; ALT_FRAME; mRNA.
DR   EMBL; BC005398; AAH05398.1; -; mRNA.
DR   CCDS; CCDS3085.1; -.
DR   PIR; T08723; T08723.
DR   RefSeq; NP_001229303.1; NM_001242374.1.
DR   RefSeq; NP_001229304.1; NM_001242375.1.
DR   RefSeq; NP_056206.1; NM_015391.3.
DR   PDB; 4UI9; EM; 3.60 A; M=1-74.
DR   PDB; 5G04; EM; 4.00 A; M=1-74.
DR   PDB; 5KHR; EM; 6.10 A; M=1-74.
DR   PDB; 5KHU; EM; 4.80 A; M=1-74.
DR   PDB; 5L9T; EM; 6.40 A; M=1-74.
DR   PDB; 5L9U; EM; 6.40 A; M=1-74.
DR   PDB; 5LCW; EM; 4.00 A; M=1-74.
DR   PDB; 6Q6G; EM; 3.20 A; M=1-74.
DR   PDB; 6Q6H; EM; 3.20 A; M=1-74.
DR   PDB; 6TLJ; EM; 3.80 A; M=1-74.
DR   PDB; 6TM5; EM; 3.90 A; M=1-74.
DR   PDBsum; 4UI9; -.
DR   PDBsum; 5G04; -.
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; Q9BS18; -.
DR   BioGRID; 117372; 76.
DR   DIP; DIP-56455N; -.
DR   IntAct; Q9BS18; 22.
DR   STRING; 9606.ENSP00000421842; -.
DR   iPTMnet; Q9BS18; -.
DR   PhosphoSitePlus; Q9BS18; -.
DR   BioMuta; ANAPC13; -.
DR   DMDM; 74732956; -.
DR   EPD; Q9BS18; -.
DR   jPOST; Q9BS18; -.
DR   MassIVE; Q9BS18; -.
DR   MaxQB; Q9BS18; -.
DR   PaxDb; Q9BS18; -.
DR   PeptideAtlas; Q9BS18; -.
DR   PRIDE; Q9BS18; -.
DR   ProteomicsDB; 78858; -.
DR   Antibodypedia; 49243; 74 antibodies.
DR   Ensembl; ENST00000354910; ENSP00000346987; ENSG00000129055.
DR   Ensembl; ENST00000510994; ENSP00000421842; ENSG00000129055.
DR   Ensembl; ENST00000511751; ENSP00000421760; ENSG00000129055.
DR   Ensembl; ENST00000514612; ENSP00000427327; ENSG00000129055.
DR   GeneID; 25847; -.
DR   KEGG; hsa:25847; -.
DR   UCSC; uc003eqi.4; human.
DR   CTD; 25847; -.
DR   DisGeNET; 25847; -.
DR   EuPathDB; HostDB:ENSG00000129055.12; -.
DR   GeneCards; ANAPC13; -.
DR   HGNC; HGNC:24540; ANAPC13.
DR   HPA; ENSG00000129055; Low tissue specificity.
DR   MIM; 614484; gene.
DR   neXtProt; NX_Q9BS18; -.
DR   OpenTargets; ENSG00000129055; -.
DR   PharmGKB; PA134949652; -.
DR   eggNOG; ENOG410J0AV; Eukaryota.
DR   eggNOG; ENOG4111UJR; LUCA.
DR   GeneTree; ENSGT00390000008673; -.
DR   HOGENOM; CLU_199969_0_0_1; -.
DR   InParanoid; Q9BS18; -.
DR   KO; K12456; -.
DR   OMA; EGWRKER; -.
DR   OrthoDB; 1635284at2759; -.
DR   PhylomeDB; Q9BS18; -.
DR   TreeFam; TF105448; -.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; Q9BS18; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 25847; 318 hits in 790 CRISPR screens.
DR   ChiTaRS; ANAPC13; human.
DR   GenomeRNAi; 25847; -.
DR   Pharos; Q9BS18; Tbio.
DR   PRO; PR:Q9BS18; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9BS18; protein.
DR   Bgee; ENSG00000129055; Expressed in nephron tubule and 235 other tissues.
DR   ExpressionAtlas; Q9BS18; baseline and differential.
DR   Genevisible; Q9BS18; HS.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
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   InterPro; IPR008401; Apc13.
DR   PANTHER; PTHR28672; PTHR28672; 1.
DR   Pfam; PF05839; Apc13p; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Mitosis; Nucleus;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..74
FT                   /note="Anaphase-promoting complex subunit 13"
FT                   /id="PRO_0000253980"
FT   CONFLICT        8
FT                   /note="D -> G (in Ref. 1; CAB43251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="E -> G (in Ref. 1; CAB43251)"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..14
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           17..20
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          34..36
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            50..53
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            63..66
FT                   /evidence="ECO:0000244|PDB:6Q6G"
SQ   SEQUENCE   74 AA;  8521 MW;  F3C52A7E3821CB3B CRC64;
     MDSEVQRDGR ILDLIDDAWR EDKLPYEDVA IPLNELPEPE QDNGGTTESV KEQEMKWTDL
     ALQYLHENVP PIGN
//
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