GenomeNet

Database: UniProt/SWISS-PROT
Entry: CDC23_BOVIN
LinkDB: CDC23_BOVIN
Original site: CDC23_BOVIN 
ID   CDC23_BOVIN             Reviewed;         597 AA.
AC   A1A4R8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   22-NOV-2017, entry version 76.
DE   RecName: Full=Cell division cycle protein 23 homolog;
DE   AltName: Full=Anaphase-promoting complex subunit 8;
DE            Short=APC8;
DE   AltName: Full=Cyclosome subunit 8;
GN   Name=CDC23; Synonyms=ANAPC8;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC       The APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation
CC       of 'Lys-11'-linked polyubiquitin chains and, to a lower extent,
CC       the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC       chains (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The mammalian APC/C is composed of 14 distinct subunits
CC       that assemble into a complex of at least 19 chains with a combined
CC       molecular mass of around 1.2 MDa. {ECO:0000250|UniProtKB:Q9UJX2}.
CC   -!- PTM: Phosphorylated. Phosphorylation on Thr-562 occurs
CC       specifically during mitosis (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the APC8/CDC23 family. {ECO:0000305}.
DR   EMBL; BC126843; AAI26844.1; -; mRNA.
DR   RefSeq; NP_001073735.1; NM_001080266.1.
DR   UniGene; Bt.1176; -.
DR   ProteinModelPortal; A1A4R8; -.
DR   SMR; A1A4R8; -.
DR   STRING; 9913.ENSBTAP00000011540; -.
DR   PaxDb; A1A4R8; -.
DR   PRIDE; A1A4R8; -.
DR   Ensembl; ENSBTAT00000011540; ENSBTAP00000011540; ENSBTAG00000008759.
DR   GeneID; 512651; -.
DR   KEGG; bta:512651; -.
DR   CTD; 8697; -.
DR   eggNOG; KOG1155; Eukaryota.
DR   eggNOG; ENOG410XPS3; LUCA.
DR   GeneTree; ENSGT00550000074886; -.
DR   HOGENOM; HOG000115852; -.
DR   InParanoid; A1A4R8; -.
DR   KO; K03355; -.
DR   OMA; MGHEFME; -.
DR   OrthoDB; EOG091G0535; -.
DR   TreeFam; TF101055; -.
DR   Reactome; R-BTA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-BTA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-BTA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-BTA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-BTA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-BTA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-BTA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-BTA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-BTA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-BTA-176412; Phosphorylation of the APC/C.
DR   Reactome; R-BTA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-BTA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-BTA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000008759; -.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; IEA:Ensembl.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
DR   Gene3D; 1.25.40.10; -; 6.
DR   InterPro; IPR007192; APC8.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF04049; ANAPC8; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Cell division; Complete proteome;
KW   Isopeptide bond; Mitosis; Phosphoprotein; Reference proteome; Repeat;
KW   TPR repeat; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q9UJX2}.
FT   CHAIN         2    597       Cell division cycle protein 23 homolog.
FT                                /FTId=PRO_0000379876.
FT   REPEAT       27     63       TPR 1.
FT   REPEAT       73    112       TPR 2.
FT   REPEAT      114    144       TPR 3.
FT   REPEAT      169    200       TPR 4.
FT   REPEAT      229    259       TPR 5.
FT   REPEAT      263    293       TPR 6.
FT   REPEAT      297    327       TPR 7.
FT   REPEAT      331    361       TPR 8.
FT   REPEAT      366    395       TPR 9.
FT   REPEAT      400    432       TPR 10.
FT   REPEAT      433    466       TPR 11.
FT   REPEAT      468    500       TPR 12.
FT   REPEAT      504    540       TPR 13.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     273    273       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     467    467       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     562    562       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     565    565       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     578    578       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     582    582       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     588    588       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     593    593       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   MOD_RES     596    596       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
FT   CROSSLNK    147    147       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9UJX2}.
SQ   SEQUENCE   597 AA;  68780 MW;  230EAF23D101564D CRC64;
     MAASSSIVSV APTASSVPVL PSSCDFSNLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF
     SLPALPLSEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD RAAHFLHGCN SKKAYFLYMY
     SRYLSGEKKK DDETVDSLGP LEKGQVKNEA LRELRVELSK KHQARELDGF GLYLYGVVLR
     KLDLVKEAID VFVEATHVLP LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE
     LQLIEEALQK YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM
     DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA ALYFQRALKL
     NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR AWYGLGQTYE ILKMPFYCLY
     YYRRAHQLRP NDSRMLVALG ECYEKLNQLV EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL
     TESEQAAQCY IKYIQDIYSC GEIVEHLEES TAFRYLAQYY FKCKLWDEAS ACAQKCCAFN
     DTREEGKALL RQILQLRNQG ETPSTEIPAP FFLPASLSAN NTPTRRVSPL NLSSVTP
//
DBGET integrated database retrieval system