ID   CCNE2_BOVIN             Reviewed;         404 AA.
AC   Q5E9K7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=G1/S-specific cyclin-E2;
GN   Name=CCNE2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the late G1
CC       and early S phase. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the CDK2 (in vivo) and CDK3 (in vitro) protein
CC       kinases to form a serine/threonine kinase holoenzyme complex. The
CC       cyclin subunit imparts substrate specificity to the complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Phosphorylation by CDK2 triggers its release from CDK2 and
CC       degradation via the ubiquitin proteasome pathway. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BT020913; AAX08930.1; -; mRNA.
DR   RefSeq; NP_001015665.1; NM_001015665.1.
DR   AlphaFoldDB; Q5E9K7; -.
DR   SMR; Q5E9K7; -.
DR   STRING; 9913.ENSBTAP00000006455; -.
DR   PaxDb; Q5E9K7; -.
DR   PRIDE; Q5E9K7; -.
DR   Ensembl; ENSBTAT00000006455; ENSBTAP00000006455; ENSBTAG00000004906.
DR   GeneID; 538436; -.
DR   KEGG; bta:538436; -.
DR   CTD; 9134; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004906; -.
DR   VGNC; VGNC:26967; CCNE2.
DR   eggNOG; KOG0655; Eukaryota.
DR   GeneTree; ENSGT00940000156934; -.
DR   HOGENOM; CLU_020695_8_0_1; -.
DR   InParanoid; Q5E9K7; -.
DR   OMA; KRHQYEI; -.
DR   OrthoDB; 993640at2759; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000004906; Expressed in pharyngeal tonsil and 104 other tissues.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0097134; C:cyclin E1-CDK2 complex; IBA:GO_Central.
DR   GO; GO:0097135; C:cyclin E2-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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl.
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   GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR   GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
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:SF70; PTHR10177:SF70; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 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..404
FT                   /note="G1/S-specific cyclin-E2"
FT                   /id="PRO_0000273976"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        6..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O96020"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O96020"
FT   MOD_RES         392
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O96020, ECO:0000305"
SQ   SEQUENCE   404 AA;  46632 MW;  C62AF31F58A1A375 CRC64;
     MSRRSSRLQA KQQPQASQTD SPQEAQIIQA KKRKTAQDVK KRKEEVTKKH QYEIRNCWPP
     VLSGGISPCI IIETPHKEIG TSDFSRFTNY RFKNLFINPS PLPDLSWGCS QDVWLNMLKK
     ETRYVHDKHF EVLHSELEPQ MRSILLDWLL EVCEVYTLHR ETFYLAQDFF DRFMLTQKDI
     NKNMLQLIGI TSLFIASKLE EIYAPKLQEF AYVTDGACSE EDILRMELAI LKALKWELCP
     VTVISWLNLF LQVDALKDAP KVLLPQYSQE KFIQIAQLLD LCILAIDSLE FQYRILAAAA
     LCHFTSIEVV KKASGLEWDN ISECVDWMVP FVSVVKSTSP AKLKIFKKIS MEDRHNIQTH
     TNYLAMLDEV NYVNTFRKEG QLSPVCNGGI MTPPKSTEKP PGKH