CDC27_MOUSE
ID CDC27_MOUSE Reviewed; 825 AA.
AC A2A6Q5; A2A6Q6; B2RXS0;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cell division cycle protein 27 homolog;
GN Name=Cdc27;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [4]
RP INTERACTION WITH FAM168B.
RX PubMed=20716133; DOI=10.1111/j.1582-4934.2010.01134.x;
RA Mishra M., Akatsu H., Heese K.;
RT "The novel protein MANI modulates neurogenesis and neurite-cone growth.";
RL J. Cell. Mol. Med. 15:1713-1725(2011).
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 (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. The mammalian APC/C is composed at least of 14
CC distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5,
CC CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13,
CC ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains
CC with a combined molecular mass of around 1.2 MDa; APC/C interacts with
CC FZR1 and FBXO5 (By similarity). Interacts with RB. Interacts with
CC FAM168B/MANI (PubMed:20716133). Interacts with MCPH1 (By similarity).
CC {ECO:0000250|UniProtKB:P30260, ECO:0000269|PubMed:20716133}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30260}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P30260}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2A6Q5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A6Q5-2; Sequence=VSP_038534, VSP_038535;
CC Name=3;
CC IsoId=A2A6Q5-3; Sequence=VSP_038534;
CC -!- PTM: Phosphorylated. Phosphorylation on Ser-427 and Thr-447 occurs
CC specifically during mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APC3/CDC27 family. {ECO:0000305}.
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DR EMBL; AL603709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34221.1; -; Genomic_DNA.
DR EMBL; BC157955; AAI57956.1; -; mRNA.
DR EMBL; BC172100; AAI72100.1; -; mRNA.
DR CCDS; CCDS36354.1; -. [A2A6Q5-1]
DR RefSeq; NP_001272917.1; NM_001285988.1. [A2A6Q5-2]
DR RefSeq; NP_663411.2; NM_145436.2. [A2A6Q5-1]
DR RefSeq; XP_006533113.1; XM_006533050.2. [A2A6Q5-3]
DR AlphaFoldDB; A2A6Q5; -.
DR SMR; A2A6Q5; -.
DR BioGRID; 229869; 8.
DR DIP; DIP-56609N; -.
DR IntAct; A2A6Q5; 4.
DR STRING; 10090.ENSMUSP00000091452; -.
DR iPTMnet; A2A6Q5; -.
DR PhosphoSitePlus; A2A6Q5; -.
DR EPD; A2A6Q5; -.
DR MaxQB; A2A6Q5; -.
DR PaxDb; A2A6Q5; -.
DR PeptideAtlas; A2A6Q5; -.
DR PRIDE; A2A6Q5; -.
DR ProteomicsDB; 280030; -. [A2A6Q5-1]
DR ProteomicsDB; 280031; -. [A2A6Q5-2]
DR ProteomicsDB; 280032; -. [A2A6Q5-3]
DR Antibodypedia; 3817; 514 antibodies from 42 providers.
DR DNASU; 217232; -.
DR Ensembl; ENSMUST00000093923; ENSMUSP00000091452; ENSMUSG00000020687. [A2A6Q5-1]
DR Ensembl; ENSMUST00000106962; ENSMUSP00000102575; ENSMUSG00000020687. [A2A6Q5-3]
DR GeneID; 217232; -.
DR KEGG; mmu:217232; -.
DR UCSC; uc007lwq.2; mouse. [A2A6Q5-1]
DR UCSC; uc007lwr.2; mouse. [A2A6Q5-2]
DR UCSC; uc011ygc.2; mouse. [A2A6Q5-3]
DR CTD; 996; -.
DR MGI; MGI:102685; Cdc27.
DR VEuPathDB; HostDB:ENSMUSG00000020687; -.
DR eggNOG; KOG1126; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_008850_1_0_1; -.
DR InParanoid; A2A6Q5; -.
DR OMA; ADKRHYN; -.
DR OrthoDB; 280620at2759; -.
DR PhylomeDB; A2A6Q5; -.
DR TreeFam; TF101058; -.
DR Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 217232; 27 hits in 74 CRISPR screens.
DR ChiTaRS; Cdc27; mouse.
DR PRO; PR:A2A6Q5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2A6Q5; protein.
DR Bgee; ENSMUSG00000020687; Expressed in undifferentiated genital tubercle and 219 other tissues.
DR ExpressionAtlas; A2A6Q5; baseline and differential.
DR Genevisible; A2A6Q5; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..825
FT /note="Cell division cycle protein 27 homolog"
FT /id="PRO_0000390473"
FT REPEAT 6..35
FT /note="TPR 1"
FT REPEAT 38..65
FT /note="TPR 2"
FT REPEAT 67..99
FT /note="TPR 3"
FT REPEAT 115..145
FT /note="TPR 4"
FT REPEAT 465..495
FT /note="TPR 5"
FT REPEAT 499..528
FT /note="TPR 6"
FT REPEAT 533..563
FT /note="TPR 7"
FT REPEAT 567..598
FT /note="TPR 8"
FT REPEAT 601..631
FT /note="TPR 9"
FT REPEAT 635..667
FT /note="TPR 10"
FT REPEAT 670..702
FT /note="TPR 11"
FT REPEAT 704..734
FT /note="TPR 12"
FT REPEAT 737..768
FT /note="TPR 13"
FT REGION 306..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30260"
FT VAR_SEQ 319
FT /note="K -> KTFCVLQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038534"
FT VAR_SEQ 461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038535"
SQ SEQUENCE 825 AA; 91842 MW; 554D8B1136826DA3 CRC64;
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL
LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ KSHDDLVTEF GDSACFTLSL
LGHVYCKTDR LAKGSECYQK SLSLNPFLWS PFESLCEIGE KPDPDQTFKL TSLQNFSSCL
PNTCTTLVSN HSLSHRQPET VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSTVI
SPDNVPLGPG TAILSKQVQN KPKTGRSLLG GPTALSPLTP SFGILPLETP SPGDGSYLQN
YTNTPSVIDV APTGAPTKKS VARMGQTGTK SVFSQSGNSR EVTPVLVAQT QSSGPQTSTT
PQVLSPTITS PPNALPRRSS RLFTSDSSTT KENSKKLKMK FPPKIPNRKT KSKTNKGGLT
QPSINDSLEI TKLDSSIISE GKITTVTPQI QAFNLQKAAA EGLMSLLREM GKGYLALCSY
NCKEAINILS HLPSHHYSTG WVLCQIGRAY FELSEYMQAE RIFSEVRRIE SFRVEGMEIY
STTLWHLQKD VALSVLSKDL TDMDKNSPEA WCAAGNCFSL QREHDIAIKF FQRAIQVDPN
YAYAYTLLGH EFVLTEELDK ALACFRNAIR VNPRHYNAWY GLGMIYYKQE KFSLAEMHFQ
KALDINPQSS VLLCHIGVVQ HALKKSEKAL DTLNKAIVID PKNPLCKFHR ASVLFANEKY
KSALQELEEL KQIVPKESLV YFLIGKVYKK LGQTHLALMN FSWAMDLDPK GANNQIKEAI
DKRYLPDDEE PITQEEQIMG TDESQESSMT DADDTQLHAA ESDEF
