ID   CCNE1_MOUSE             Reviewed;         408 AA.
AC   Q61457; Q05BA1; Q05BA6; Q05BB7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=G1/S-specific cyclin-E1;
GN   Name=Ccne1; Synonyms=Ccne;
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 [MRNA].
RC   STRAIN=129/J;
RX   PubMed=8003041; DOI=10.1006/bbrc.1994.1800;
RA   Damjanov I., Shan J., Wang R.F., Damjanov A., Deloia J.A.;
RT   "Molecular cloning and characterization of murine cyclin E.";
RL   Biochem. Biophys. Res. Commun. 201:994-1000(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Limb;
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   IDENTIFICATION IN A COMPLEX WITH CDK2; CCNA1 AND CABLES1.
RX   PubMed=11585773;
RA   Wu C.-L., Kirley S.D., Xiao H., Chuang Y., Chung D.C., Zukerberg L.R.;
RT   "Cables enhances cdk2 tyrosine 15 phosphorylation by Wee1, inhibits cell
RT   growth, and is lost in many human colon and squamous cancers.";
RL   Cancer Res. 61:7325-7332(2001).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC       (start) transition.
CC   -!- SUBUNIT: Interacts with CDK2 protein kinase to form a serine/threonine
CC       kinase holoenzyme complex. The cyclin subunit imparts substrate
CC       specificity to the complex. Part of a complex consisting of UHRF2, CDK2
CC       and CCNE1. Interacts directly with UHRF2; the interaction ubiquitinates
CC       CCNE1 and appears to occur independently of CCNE1 phosphorylation (By
CC       similarity). Found in a complex with CDK2, CABLES1 and CCNA1
CC       (PubMed:11585773). Interacts with INCA1 (By similarity).
CC       {ECO:0000250|UniProtKB:P24864, ECO:0000269|PubMed:11585773}.
CC   -!- INTERACTION:
CC       Q61457; P11440: Cdk1; NbExp=3; IntAct=EBI-643090, EBI-846949;
CC       Q61457; P97377: Cdk2; NbExp=3; IntAct=EBI-643090, EBI-847048;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24864}.
CC   -!- TISSUE SPECIFICITY: Found in adult spleen, and to a lesser extent in
CC       adult testis and brain.
CC   -!- PTM: Phosphorylation of both Thr-393 by GSK3 and Ser-397 by CDK2
CC       creates a high affinity degron recognized by FBXW7, and accelerates
CC       degradation via the ubiquitin proteasome pathway. Phosphorylation at
CC       Thr-74 creates a low affinity degron also recognized by FBXW7 (By
CC       similarity). {ECO:0000250|UniProtKB:P24864}.
CC   -!- PTM: Ubiquitinated by UHRF2; appears to occur independently of
CC       phosphorylation. {ECO:0000250|UniProtKB:P24864}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA53482.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X75888; CAA53482.1; ALT_FRAME; mRNA.
DR   EMBL; BC062152; AAH62152.1; -; mRNA.
DR   EMBL; BC084588; AAH84588.1; -; mRNA.
DR   EMBL; BC106191; AAI06192.1; -; mRNA.
DR   CCDS; CCDS39914.1; -.
DR   PIR; JC2497; JC2497.
DR   RefSeq; NP_031659.2; NM_007633.2.
DR   AlphaFoldDB; Q61457; -.
DR   SMR; Q61457; -.
DR   BioGRID; 198552; 11.
DR   ComplexPortal; CPX-2081; Cyclin E1-CDK2 complex.
DR   DIP; DIP-45868N; -.
DR   ELM; Q61457; -.
DR   IntAct; Q61457; 3.
DR   MINT; Q61457; -.
DR   STRING; 10090.ENSMUSP00000103658; -.
DR   iPTMnet; Q61457; -.
DR   PhosphoSitePlus; Q61457; -.
DR   EPD; Q61457; -.
DR   MaxQB; Q61457; -.
DR   PaxDb; 10090-ENSMUSP00000103658; -.
DR   ProteomicsDB; 281252; -.
DR   Pumba; Q61457; -.
DR   Antibodypedia; 3286; 1363 antibodies from 48 providers.
DR   DNASU; 12447; -.
DR   Ensembl; ENSMUST00000108023.10; ENSMUSP00000103658.4; ENSMUSG00000002068.17.
DR   GeneID; 12447; -.
DR   KEGG; mmu:12447; -.
DR   UCSC; uc009gkr.1; mouse.
DR   AGR; MGI:88316; -.
DR   CTD; 898; -.
DR   MGI; MGI:88316; Ccne1.
DR   VEuPathDB; HostDB:ENSMUSG00000002068; -.
DR   eggNOG; KOG0655; Eukaryota.
DR   GeneTree; ENSGT00940000156256; -.
DR   HOGENOM; CLU_020695_8_0_1; -.
DR   InParanoid; Q61457; -.
DR   OMA; HRIQTHV; -.
DR   OrthoDB; 5474295at2759; -.
DR   PhylomeDB; Q61457; -.
DR   TreeFam; TF101005; -.
DR   Reactome; R-MMU-1538133; G0 and Early G1.
DR   Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR   Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-MMU-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR   Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR   Reactome; R-MMU-69563; p53-Dependent G1 DNA Damage Response.
DR   Reactome; R-MMU-8849470; PTK6 Regulates Cell Cycle.
DR   Reactome; R-MMU-9706019; RHOBTB3 ATPase cycle.
DR   BioGRID-ORCS; 12447; 5 hits in 82 CRISPR screens.
DR   ChiTaRS; Ccne1; mouse.
DR   PRO; PR:Q61457; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q61457; Protein.
DR   Bgee; ENSMUSG00000002068; Expressed in ectoplacental cone and 242 other cell types or tissues.
DR   ExpressionAtlas; Q61457; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0097134; C:cyclin E1-CDK2 complex; IDA:MGI.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:MGI.
DR   GO; GO:0016301; F:kinase activity; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IGI:MGI.
DR   GO; GO:0006270; P:DNA replication initiation; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:0007129; P:homologous chromosome pairing at meiosis; IGI:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR   GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; ISO:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   GO; GO:0032880; P:regulation of protein localization; IGI:MGI.
DR   GO; GO:0000723; P:telomere maintenance; IGI:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR   CDD; cd20581; CYCLIN_CCNE1_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF71; G1_S-SPECIFIC CYCLIN-E1; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
DR   Genevisible; Q61457; MM.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..408
FT                   /note="G1/S-specific cyclin-E1"
FT                   /id="PRO_0000080450"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         74
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
FT   MOD_RES         393
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
FT   MOD_RES         397
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
FT   CONFLICT        2
FT                   /note="P -> Q (in Ref. 2; AAH84588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="H -> Q (in Ref. 1; CAA53482 and 2;
FT                   AAH62152/AAH84588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290..291
FT                   /note="LE -> FR (in Ref. 2; AAH62152)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   408 AA;  46986 MW;  4916B5D7117ADA69 CRC64;
     MPRERDSTDH SNMKEEGGSD LSVRSRKRKA NVAVFLQDPD EEIAKIDKTV KSEDSSQPWD
     DNSACVDPCS FIPTPNKEED NELEYPRTAF QPRKIRPPRA SPLPVLNWGN REEVWRIMLN
     KEKTYLRDEH FLQRHPLLQA RMRAVLLDWL MEVCEVYKLH RETFYLAQDF FDRYMASQHN
     IIKTLLQLIG ISALFIASKL EEIYPPKLHQ FAYVTDGACS GDEILTMELM MMKALKWRLS
     PLTIVSWLNV YVQVAYVNDT GEVLMPQYPQ QVFVQIAELL DLCVLDVGCL EFPYGVLAAS
     ALYHFSSLEL MQKVSGYQWC DIEKCVKWMV PFAMVIREMG SSKLKHFRGV PMEDSHNIQT
     HTNSLDLLDK AQAKKAILSE QNRISPPPSV VLTPPPSSKK QSSEQETE
//