ID   CCNE2_XENLA             Reviewed;         408 AA.
AC   Q91780;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=G1/S-specific cyclin-E2;
DE   AltName: Full=Cyclin-E-1;
GN   Name=cyce2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7896832; DOI=10.1074/jbc.270.12.6843;
RA   Rempel R.E., Sleight S.B., Maller J.L.;
RT   "Maternal Xenopus Cdk2-cyclin E complexes function during meiotic and early
RT   embryonic cell cycles that lack a G1 phase.";
RL   J. Biol. Chem. 270:6843-6855(1995).
RN   [2]
RP   NUCLEAR LOCALIZATION SIGNAL.
RX   PubMed=12475960; DOI=10.1091/mbc.e02-07-0449;
RA   Moore J.D., Kornbluth S., Hunt T.;
RT   "Identification of the nuclear localization signal in Xenopus cyclin E and
RT   analysis of its role in replication and mitosis.";
RL   Mol. Biol. Cell 13:4388-4400(2002).
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; L23857; AAA73524.1; -; mRNA.
DR   PIR; A56186; A56186.
DR   AlphaFoldDB; Q91780; -.
DR   SMR; Q91780; -.
DR   Proteomes; UP000186698; Genome assembly.
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..408
FT                   /note="G1/S-specific cyclin-E2"
FT                   /id="PRO_0000080455"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           24..29
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:12475960"
FT   COMPBIAS        385..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         394
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
SQ   SEQUENCE   408 AA;  47172 MW;  940C3652298671F5 CRC64;
     MPVISNPAVE KSTKDEGTAS CSVRSRKRKA DVTIFLQDPD ETLDSLEMTK KKQYQDRGPW
     SNEMTCKSPH KLIPTPEKEE HEPNPTNYSH FASLRFSPVS VSPLPRLGWA NQDDVWRNML
     NKDRIYLRDK NFFQKHPQLQ PNMRAILLDW LMEVCEVYKL HRETFYLAQD FFDRFMATQK
     NVIKSRLQLI GITSLFIAAK LEEIYPPKLH QFSFITDGAC TEDEITRMEL IIMKDLGWCL
     SPMTIVSWFN VFLQVAYIRE LQQFLRPQFP QEIYIQIVQL LDLCVLDICC LEYPYGVLAA
     SAMYHFSCPE LVEKVSGFKV TELQGCIKWL VPFAMAIKEG GKSKLNFFKG VDIEDAHNIQ
     THSGCLELME KVYINQALLE EQNRTSPIPT GVLTPPQSNK KQKSDRAD