ID   CCNE1_DANRE             Reviewed;         410 AA.
AC   P47794;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=G1/S-specific cyclin-E1;
GN   Name=ccne1; Synonyms=ccne, cyce;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9019240;
RX   DOI=10.1002/(sici)1097-0177(199605)206:1<1::aid-aja1>3.0.co;2-m;
RA   Yarden A., Geiger B.;
RT   "Zebrafish cyclin E regulation during early embryogenesis.";
RL   Dev. Dyn. 206:1-11(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:P24864}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24864}.
CC   -!- PTM: Phosphorylation by CDK2 triggers its release from CDK2 and
CC       degradation via the ubiquitin proteasome pathway.
CC       {ECO:0000250|UniProtKB:P24864}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X83594; CAA58574.1; -; mRNA.
DR   EMBL; BC045842; AAH45842.1; -; mRNA.
DR   EMBL; BC075747; AAH75747.1; -; mRNA.
DR   PIR; S52288; S52288.
DR   RefSeq; NP_571070.1; NM_130995.1.
DR   AlphaFoldDB; P47794; -.
DR   SMR; P47794; -.
DR   STRING; 7955.ENSDARP00000024696; -.
DR   PaxDb; P47794; -.
DR   PRIDE; P47794; -.
DR   GeneID; 30188; -.
DR   KEGG; dre:30188; -.
DR   CTD; 898; -.
DR   ZFIN; ZDB-GENE-980526-168; ccne1.
DR   eggNOG; KOG0655; Eukaryota.
DR   InParanoid; P47794; -.
DR   OrthoDB; 993640at2759; -.
DR   PhylomeDB; P47794; -.
DR   Reactome; R-DRE-1538133; G0 and Early G1.
DR   Reactome; R-DRE-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-DRE-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; R-DRE-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR   Reactome; R-DRE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DRE-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR   Reactome; R-DRE-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-DRE-69231; Cyclin D associated events in G1.
DR   Reactome; R-DRE-69563; p53-Dependent G1 DNA Damage Response.
DR   Reactome; R-DRE-8849470; PTK6 Regulates Cell Cycle.
DR   Reactome; R-DRE-9706019; RHOBTB3 ATPase cycle.
DR   PRO; PR:P47794; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0097134; C:cyclin E1-CDK2 complex; IBA:GO_Central.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0016301; F:kinase activity; IDA:ZFIN.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR028858; Cyclin_E.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   PANTHER; PTHR10177:SF71; PTHR10177:SF71; 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; SSF47954; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..410
FT                   /note="G1/S-specific cyclin-E1"
FT                   /id="PRO_0000080453"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         397
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
SQ   SEQUENCE   410 AA;  46631 MW;  2760F1CD30214077 CRC64;
     MPSKKVLQTE HINTTDEAPK TTSVRPRKRK ADVAIHLQDP DEEVTEMTRK KQCASQACWN
     PDTGYTSPCR RIPTPDEVEE PVAFGSVGFT QYASESIFIT PTRSTPLPAL CWASKDEVWN
     NLLGKDKLYL RDTRVMERHP NLQPKMRAIL LDWLMEVCEV YKLHRETFYL GQDYFDRFMA
     TQENVLKTTL QLIGISCLFI AAKMEEIYPP KVHQFAYVTD GACTEDDILS MEIIIMKELN
     WSLSPLTPVA WLNIYMQMAY LKETAEVLTA QYPQATFVQI AELLDLCILD VRSLEFSYSL
     LAASALFHFS SLELVIKVSG LKWCDLEECV RWMVPFAMSI REAGSSALKT FKGIAADDMH
     NIQTHVPYLE WLGKVHSYQL VDIESSQRSP VPTGVLTPPP SSEKPESTIS