ID   CCNE1_CHICK             Reviewed;         407 AA.
AC   P49707; Q91032;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=G1/S-specific cyclin-E1;
GN   Name=CCNE1; Synonyms=CCNE;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Li H., Lahti J.M., Valentine M., Houston J., Kidd V.J.;
RT   "The cyclin E gene is apparently essential in avian B cells.";
RL   Submitted (JUN-1995) 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 (By similarity).
CC       {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; U28981; AAA74981.1; -; mRNA.
DR   EMBL; AH003231; AAA81647.1; -; Genomic_DNA.
DR   RefSeq; NP_001026529.1; NM_001031358.1.
DR   AlphaFoldDB; P49707; -.
DR   SMR; P49707; -.
DR   STRING; 9031.ENSGALP00000007147; -.
DR   PaxDb; P49707; -.
DR   GeneID; 426117; -.
DR   KEGG; gga:426117; -.
DR   CTD; 898; -.
DR   VEuPathDB; HostDB:geneid_426117; -.
DR   eggNOG; KOG0655; Eukaryota.
DR   InParanoid; P49707; -.
DR   OrthoDB; 993640at2759; -.
DR   PhylomeDB; P49707; -.
DR   PRO; PR:P49707; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
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..407
FT                   /note="G1/S-specific cyclin-E1"
FT                   /id="PRO_0000080452"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         392
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
FT   CONFLICT        106
FT                   /note="G -> GD (in Ref. 1; AAA81647)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="L -> S (in Ref. 1; AAA81647)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  46739 MW;  A1032C7CB0BC1D1A CRC64;
     MRRESDCAEE KAPAKGEGGA EGTVRARKRK ADVATFLQDP DEEIAKIEMS RKKQYENQLS
     WNNINKDPHM LIPTPDKDDD PVGVDYSHFI HLNVASTRSS PLPILGWANR DDVWKNMINK
     EETYVRDKLY MQRHPLLQPK MRTILLDWLM EVCEVYKLYR ETFYLAQDFF DRFMATQQNV
     VKTLLQLIGI SSLFIAAKLE EIYPPKLHQF AYVTDGACTE DEILSMELII MKALNWNLNP
     LTVVSWLNIY MQVAYLNELY EVLLPQYPQQ IFVQIAELLD LCVLDIGCLE YTYGVLAASA
     LYHFSSSELM QKVSGYEWCE IEECVKWMVP FAMAIREVGS SKLKHFRGIA PEDLHNIQTH
     INSLDLLDKA QAKQAILAEQ NRTSPFPTGV LTPPQSSKKQ PAGLKPI